FAS2_YEAST
ID FAS2_YEAST Reviewed; 1887 AA.
AC P19097; D6W3D9; Q12533;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Fatty acid synthase subunit alpha;
DE EC=2.3.1.86;
DE Includes:
DE RecName: Full=Acyl carrier;
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE EC=1.1.1.100;
DE AltName: Full=Beta-ketoacyl reductase;
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
DE EC=2.3.1.41;
DE AltName: Full=Beta-ketoacyl synthase;
GN Name=FAS2; OrderedLocusNames=YPL231W; ORFNames=P1409;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2900835; DOI=10.1016/s0021-9258(18)37757-3;
RA Mohamed A.H., Chirala S.S., Mody N.H., Huang W.Y., Wakil S.J.;
RT "Primary structure of the multifunctional alpha subunit protein of yeast
RT fatty acid synthase derived from FAS2 gene sequence.";
RL J. Biol. Chem. 263:12315-12325(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26786 / X2180-1A;
RA Schueller H.-J.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP MUTAGENESIS OF GLY-1250.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8041367; DOI=10.1007/bf00280191;
RA Inokoshi J., Tomoda H., Hashimoto H., Watanabe A., Takeshima H., Omura S.;
RT "Cerulenin-resistant mutants of Saccharomyces cerevisiae with an altered
RT fatty acid synthase gene.";
RL Mol. Gen. Genet. 244:90-96(1994).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-958 AND SER-1440, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-37, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 671-1744 IN COMPLEX WITH FAS1, AND
RP SUBUNIT.
RX PubMed=17448991; DOI=10.1016/j.cell.2007.03.013;
RA Lomakin I.B., Xiong Y., Steitz T.A.;
RT "The crystal structure of yeast fatty acid synthase, a cellular machine
RT with eight active sites working together.";
RL Cell 129:319-332(2007).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH FAS1, SUBUNIT, AND
RP PHOSPHOPANTETHEINYLATION AT SER-180.
RX PubMed=17431182; DOI=10.1126/science.1138249;
RA Leibundgut M., Jenni S., Frick C., Ban N.;
RT "Structural basis for substrate delivery by acyl carrier protein in the
RT yeast fatty acid synthase.";
RL Science 316:288-290(2007).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) IN COMPLEX WITH FAS1 AND THE
RP INHIBITOR CERULENIN, AND ACTIVITY REGULATION.
RX PubMed=18725634; DOI=10.1073/pnas.0805827105;
RA Johansson P., Wiltschi B., Kumari P., Kessler B., Vonrhein C., Vonck J.,
RA Oesterhelt D., Grininger M.;
RT "Inhibition of the fungal fatty acid synthase type I multienzyme complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12803-12808(2008).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1766-1887 IN COMPLEX WITH FAS1 AND
RP ACETYL-COA, MUTAGENESIS OF VAL-1769; GLY-1770; VAL-1771; ASP-1772;
RP VAL-1773; GLU-1774; ARG-1841; VAL-1879 AND VAL-1881, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=19679086; DOI=10.1016/j.str.2009.06.014;
RA Johansson P., Mulinacci B., Koestler C., Vollrath R., Oesterhelt D.,
RA Grininger M.;
RT "Multimeric options for the auto-activation of the Saccharomyces cerevisiae
RT FAS type I megasynthase.";
RL Structure 17:1063-1074(2009).
CC -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain
CC fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit
CC contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-
CC protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This
CC subunit coordinates the binding of the six beta subunits to the enzyme
CC complex.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83139; EC=2.3.1.86;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC -!- ACTIVITY REGULATION: Inhibited by cerulenin by covalent binding to
CC active site of the ketoacyl synthase (KS) region.
CC {ECO:0000269|PubMed:18725634}.
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000269|PubMed:17431182,
CC ECO:0000269|PubMed:17448991, ECO:0000269|PubMed:18725634,
CC ECO:0000269|PubMed:19679086}.
CC -!- INTERACTION:
CC P19097; P07149: FAS1; NbExp=9; IntAct=EBI-6806, EBI-6795;
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of the Acyl carrier domain by the C-terminal PPT domain. This
CC modification is essential for activity because fatty acids are bound in
CC thioester linkage to the sulfhydryl of the prosthetic group.
CC -!- MISCELLANEOUS: Present with 17000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC synthetase subunit alpha family. {ECO:0000305}.
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DR EMBL; J03936; AAA34601.1; -; Genomic_DNA.
DR EMBL; X76890; CAA54218.1; -; Genomic_DNA.
DR EMBL; X94561; CAA64256.1; -; Genomic_DNA.
DR EMBL; Z73586; CAA97947.1; -; Genomic_DNA.
DR EMBL; Z73587; CAA97948.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11205.1; -; Genomic_DNA.
DR PIR; S61703; S61703.
DR RefSeq; NP_015093.1; NM_001184045.1.
DR PDB; 2ML8; NMR; -; A=138-302.
DR PDB; 2PFF; X-ray; 4.00 A; A/D/G=671-1744.
DR PDB; 2UV8; X-ray; 3.10 A; A/B/C=1-1887.
DR PDB; 2VKZ; X-ray; 4.00 A; A/B/C=1-1887.
DR PDB; 2WAS; X-ray; 1.90 A; A/B/C/D/E/F=1766-1887.
DR PDB; 2WAT; X-ray; 2.20 A; A/B/C/D/E/F=1766-1887.
DR PDB; 3HMJ; X-ray; 4.00 A; A/B/C=1-1887.
DR PDB; 6JSH; EM; 5.10 A; C/H/I=1443-1513.
DR PDB; 6JSI; EM; 4.70 A; C/H/I=1443-1513.
DR PDB; 6QL5; EM; 2.80 A; A/B/C/D/E/F=1-1887.
DR PDB; 6QL6; EM; 2.90 A; A/B/C/D/E/F=1-1887.
DR PDB; 6QL7; X-ray; 4.60 A; A/B/C/D/E/F/a/b/c/d/e/f=1-1887.
DR PDB; 6QL9; X-ray; 2.82 A; A/B/C/D/E/F=1-1887.
DR PDB; 6TA1; EM; 3.10 A; A/B/D/F/I/K=1-1887.
DR PDB; 6WC7; EM; 5.80 A; A=1-1887.
DR PDBsum; 2ML8; -.
DR PDBsum; 2PFF; -.
DR PDBsum; 2UV8; -.
DR PDBsum; 2VKZ; -.
DR PDBsum; 2WAS; -.
DR PDBsum; 2WAT; -.
DR PDBsum; 3HMJ; -.
DR PDBsum; 6JSH; -.
DR PDBsum; 6JSI; -.
DR PDBsum; 6QL5; -.
DR PDBsum; 6QL6; -.
DR PDBsum; 6QL7; -.
DR PDBsum; 6QL9; -.
DR PDBsum; 6TA1; -.
DR PDBsum; 6WC7; -.
DR AlphaFoldDB; P19097; -.
DR BMRB; P19097; -.
DR SMR; P19097; -.
DR BioGRID; 35931; 412.
DR ComplexPortal; CPX-1162; Fatty-acyl-CoA synthase.
DR DIP; DIP-960N; -.
DR IntAct; P19097; 20.
DR MINT; P19097; -.
DR STRING; 4932.YPL231W; -.
DR iPTMnet; P19097; -.
DR MaxQB; P19097; -.
DR PaxDb; P19097; -.
DR PRIDE; P19097; -.
DR TopDownProteomics; P19097; -.
DR EnsemblFungi; YPL231W_mRNA; YPL231W; YPL231W.
DR GeneID; 855845; -.
DR KEGG; sce:YPL231W; -.
DR SGD; S000006152; FAS2.
DR VEuPathDB; FungiDB:YPL231W; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR GeneTree; ENSGT00940000176444; -.
DR HOGENOM; CLU_000114_0_0_1; -.
DR InParanoid; P19097; -.
DR OMA; QYHIDHC; -.
DR BioCyc; MetaCyc:YPL231W-MON; -.
DR BioCyc; YEAST:YPL231W-MON; -.
DR BRENDA; 2.3.1.86; 984.
DR SABIO-RK; P19097; -.
DR EvolutionaryTrace; P19097; -.
DR PRO; PR:P19097; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P19097; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005835; C:fatty acid synthase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IDA:SGD.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IMP:SGD.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IMP:SGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IDA:ComplexPortal.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; -; 1.
DR HAMAP; MF_00101; AcpS; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR002582; ACPS.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR026025; FAS_alpha_yeast.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR SUPFAM; SSF56214; SSF56214; 1.
DR TIGRFAMs; TIGR00556; pantethn_trn; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Isopeptide bond; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Multifunctional enzyme; NAD; NADP; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation.
FT CHAIN 1..1887
FT /note="Fatty acid synthase subunit alpha"
FT /id="PRO_0000180287"
FT DOMAIN 145..220
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 96..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..874
FT /note="Beta-ketoacyl reductase"
FT REGION 1149..1363
FT /note="Beta-ketoacyl synthase"
FT ACT_SITE 1305
FT /note="For beta-ketoacyl synthase activity"
FT BINDING 1772..1774
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 1772
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 1773
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 1774
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 1798
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:19679086"
FT BINDING 1808
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:19679086"
FT BINDING 1817..1827
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 1841..1844
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 1871..1873
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 1872
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 1873
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 180
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:17431182"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 958
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 1440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 1250
FT /note="G->S: Cerulenin-resistance."
FT /evidence="ECO:0000269|PubMed:8041367"
FT MUTAGEN 1769
FT /note="V->D: Does not affect oligomerization; when
FT associated with S-1771 and L-1773 or S-1771; L-1773; S-1879
FT and E-1881."
FT /evidence="ECO:0000269|PubMed:19679086"
FT MUTAGEN 1770
FT /note="G->D: Loss of transferase activity."
FT /evidence="ECO:0000269|PubMed:19679086"
FT MUTAGEN 1771
FT /note="V->S: Does not affect oligomerization but lacks
FT transferase activity; when associated with D-1769 and L-
FT 1773 or D-1769; L-1773; S-1879 and E-1881."
FT /evidence="ECO:0000269|PubMed:19679086"
FT MUTAGEN 1772
FT /note="D->S: Loss of transferase activity; when associated
FT with S-1774."
FT /evidence="ECO:0000269|PubMed:19679086"
FT MUTAGEN 1773
FT /note="V->L: Does not affect oligomerization but lacks
FT transferase activity; when associated with D-1769 and S-
FT 1771 or D-1769; S-1771; S-1879 and E-1881."
FT /evidence="ECO:0000269|PubMed:19679086"
FT MUTAGEN 1774
FT /note="E->S: Loss of transferase activity; when associated
FT with S-1772."
FT /evidence="ECO:0000269|PubMed:19679086"
FT MUTAGEN 1841
FT /note="R->A: Loss off transferase activity."
FT /evidence="ECO:0000269|PubMed:19679086"
FT MUTAGEN 1879
FT /note="V->S: Does not affect oligomerization but lacks
FT transferase activity; when associated with D-1769; S-1771;
FT L-1773 and E-1881."
FT /evidence="ECO:0000269|PubMed:19679086"
FT MUTAGEN 1881
FT /note="V->E: Does not affect oligomerization but lacks
FT transferase activity; when associated with D-1769; S-1771;
FT L-1773 and S-1879."
FT /evidence="ECO:0000269|PubMed:19679086"
FT CONFLICT 310
FT /note="G -> GTTGTGG (in Ref. 1; AAA34601)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="T -> I (in Ref. 1; AAA34601)"
FT /evidence="ECO:0000305"
FT CONFLICT 941..1019
FT /note="AKLRKELVETSEVRKAVSIETALEHKVVNGNSADAAYAQVEIQPRANIQLDF
FT PELKPYKQVKQIAPAELEGLLDLERVI -> CLNCVKSWLKLLKLERQFPSKLLWSIRL
FT SMAIALMLHMLKSKFNQELTFNWTSQNRNHTNRLNKLLPLSLRVCWIWKELF (in
FT Ref. 1; AAA34601)"
FT /evidence="ECO:0000305"
FT CONFLICT 1036..1041
FT /note="RWEMEA -> KMGNGS (in Ref. 1; AAA34601)"
FT /evidence="ECO:0000305"
FT CONFLICT 1408
FT /note="A -> S (in Ref. 1; AAA34601)"
FT /evidence="ECO:0000305"
FT CONFLICT 1671
FT /note="N -> T (in Ref. 1; AAA34601)"
FT /evidence="ECO:0000305"
FT HELIX 3..20
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:2ML8"
FT HELIX 280..298
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 329..350
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 356..382
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 384..389
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 405..421
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 430..440
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 445..456
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 464..483
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 497..503
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 509..515
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 522..531
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 605..607
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 609..615
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 626..629
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 637..643
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 653..668
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 688..698
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 702..709
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 712..725
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 731..736
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 742..753
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 756..759
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 766..770
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 781..783
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 786..795
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 797..811
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 812..814
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 820..826
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 839..845
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 846..848
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 849..855
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 859..861
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 862..869
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 885..889
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 898..906
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 907..909
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 911..919
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 922..927
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 930..932
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 933..935
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 936..968
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 971..976
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 998..1004
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1007..1009
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 1010..1012
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1015..1017
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1019..1028
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1033..1042
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1047..1056
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1059..1067
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1070..1077
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 1078..1080
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1086..1088
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1089..1099
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1101..1105
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1108..1111
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1118..1126
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1134..1136
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1138..1148
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1149..1151
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1152..1156
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 1158..1160
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1163..1167
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1172..1179
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1185..1187
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 1195..1199
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1202..1207
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1210..1225
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1231..1233
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1234..1237
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1240..1242
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1243..1245
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1248..1251
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1254..1261
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 1262..1267
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1274..1278
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1282..1290
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1304..1306
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1307..1320
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1325..1333
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1337..1345
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1352..1357
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1362..1364
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1381..1389
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1390..1396
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1402..1410
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1424..1429
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1441..1443
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1445..1474
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1483..1508
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 1512..1515
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1517..1519
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1521..1527
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 1528..1530
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1533..1535
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1536..1540
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1547..1564
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1572..1575
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1578..1581
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1585..1587
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1588..1600
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1612..1614
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1616..1620
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1638..1645
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 1646..1648
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1649..1656
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1659..1662
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1667..1693
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1708..1710
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1711..1716
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1726..1728
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1730..1732
FT /evidence="ECO:0007829|PDB:2UV8"
FT TURN 1735..1739
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 1742..1745
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1769..1775
FT /evidence="ECO:0007829|PDB:2WAS"
FT HELIX 1776..1778
FT /evidence="ECO:0007829|PDB:2WAS"
FT HELIX 1784..1790
FT /evidence="ECO:0007829|PDB:2WAS"
FT HELIX 1793..1800
FT /evidence="ECO:0007829|PDB:2WAS"
FT STRAND 1802..1804
FT /evidence="ECO:0007829|PDB:2WAS"
FT HELIX 1805..1823
FT /evidence="ECO:0007829|PDB:2WAS"
FT STRAND 1837..1842
FT /evidence="ECO:0007829|PDB:2WAS"
FT STRAND 1845..1851
FT /evidence="ECO:0007829|PDB:2WAS"
FT HELIX 1853..1860
FT /evidence="ECO:0007829|PDB:2WAS"
FT TURN 1861..1863
FT /evidence="ECO:0007829|PDB:2WAS"
FT STRAND 1866..1873
FT /evidence="ECO:0007829|PDB:2WAS"
FT STRAND 1875..1885
FT /evidence="ECO:0007829|PDB:2WAS"
SQ SEQUENCE 1887 AA; 206947 MW; 08B872734CF3AEEA CRC64;
MKPEVEQELA HILLTELLAY QFASPVRWIE TQDVFLKDFN TERVVEIGPS PTLAGMAQRT
LKNKYESYDA ALSLHREILC YSKDAKEIYY TPDPSELAAK EEPAKEEAPA PTPAASAPAP
AAAAPAPVAA AAPAAAAAEI ADEPVKASLL LHVLVAHKLK KSLDSIPMSK TIKDLVGGKS
TVQNEILGDL GKEFGTTPEK PEETPLEELA ETFQDTFSGA LGKQSSSLLS RLISSKMPGG
FTITVARKYL QTRWGLPSGR QDGVLLVALS NEPAARLGSE ADAKAFLDSM AQKYASIVGV
DLSSAASASG AAGAGAAAGA AMIDAGALEE ITKDHKVLAR QQLQVLARYL KMDLDNGERK
FLKEKDTVAE LQAQLDYLNA ELGEFFVNGV ATSFSRKKAR TFDSSWNWAK QSLLSLYFEI
IHGVLKNVDR EVVSEAINIM NRSNDALIKF MEYHISNTDE TKGENYQLVK TLGEQLIENC
KQVLDVDPVY KDVAKPTGPK TAIDKNGNIT YSEEPREKVR KLSQYVQEMA LGGPITKESQ
PTIEEDLTRV YKAISAQADK QDISSSTRVE FEKLYSDLMK FLESSKEIDP SQTTQLAGMD
VEDALDKDST KEVASLPNKS TISKTVSSTI PRETIPFLHL RKKTPAGDWK YDRQLSSLFL
DGLEKAAFNG VTFKDKYVLI TGAGKGSIGA EVLQGLLQGG AKVVVTTSRF SKQVTDYYQS
IYAKYGAKGS TLIVVPFNQG SKQDVEALIE FIYDTEKNGG LGWDLDAIIP FAAIPEQGIE
LEHIDSKSEF AHRIMLTNIL RMMGCVKKQK SARGIETRPA QVILPMSPNH GTFGGDGMYS
ESKLSLETLF NRWHSESWAN QLTVCGAIIG WTRGTGLMSA NNIIAEGIEK MGVRTFSQKE
MAFNLLGLLT PEVVELCQKS PVMADLNGGL QFVPELKEFT AKLRKELVET SEVRKAVSIE
TALEHKVVNG NSADAAYAQV EIQPRANIQL DFPELKPYKQ VKQIAPAELE GLLDLERVIV
VTGFAEVGPW GSARTRWEME AFGEFSLEGC VEMAWIMGFI SYHNGNLKGR PYTGWVDSKT
KEPVDDKDVK AKYETSILEH SGIRLIEPEL FNGYNPEKKE MIQEVIVEED LEPFEASKET
AEQFKHQHGD KVDIFEIPET GEYSVKLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI
SDDIISQVDP ITLFVLVSVV EAFIASGITD PYEMYKYVHV SEVGNCSGSG MGGVSALRGM
FKDRFKDEPV QNDILQESFI NTMSAWVNML LISSSGPIKT PVGACATSVE SVDIGVETIL
SGKARICIVG GYDDFQEEGS FEFGNMKATS NTLEEFEHGR TPAEMSRPAT TTRNGFMEAQ
GAGIQIIMQA DLALKMGVPI YGIVAMAATA TDKIGRSVPA PGKGILTTAR EHHSSVKYAS
PNLNMKYRKR QLVTREAQIK DWVENELEAL KLEAEEIPSE DQNEFLLERT REIHNEAESQ
LRAAQQQWGN DFYKRDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND KNESATINEM
MKHLGRSEGN PVIGVFQKFL TGHPKGAAGA WMMNGALQIL NSGIIPGNRN ADNVDKILEQ
FEYVLYPSKT LKTDGVRAVS ITSFGFGQKG GQAIVVHPDY LYGAITEDRY NEYVAKVSAR
EKSAYKFFHN GMIYNKLFVS KEHAPYTDEL EEDVYLDPLA RVSKDKKSGS LTFNSKNIQS
KDSYINANTI ETAKMIENMT KEKVSNGGVG VDVELITSIN VENDTFIERN FTPQEIEYCS
AQPSVQSSFA GTWSAKEAVF KSLGVKSLGG GAALKDIEIV RVNKNAPAVE LHGNAKKAAE
EAGVTDVKVS ISHDDLQAVA VAVSTKK
