PGK_YEAST
ID PGK_YEAST Reviewed; 416 AA.
AC P00560; D6VR21;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=PGK1; OrderedLocusNames=YCR012W; ORFNames=YCR12W;
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=6296791; DOI=10.1093/nar/10.23.7791;
RA Hitzeman R.A., Hagie F.E., Hayflick J.S., Chen C.Y., Seeburg P.H.,
RA Derynck R.;
RT "The primary structure of the Saccharomyces cerevisiae gene for 3-
RT phosphoglycerate kinase.";
RL Nucleic Acids Res. 10:7791-7808(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1626432; DOI=10.1002/yea.320080508;
RA Skala J., Purnelle B., Goffeau A.;
RT "The complete sequence of a 10.8 kb segment distal of SUF2 on the right arm
RT of chromosome III from Saccharomyces cerevisiae reveals seven open reading
RT frames including the RVS161, ADP1 and PGK genes.";
RL Yeast 8:409-417(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 PROTEIN SEQUENCE OF 173-202 AND 238-270.
RX PubMed=7287307; DOI=10.1111/j.1399-3011.1981.tb02006.x;
RA Fattoum A., Roustan C., Karoui D., Feinberg J., Pradel L.-A., Gregoire J.,
RA Rochat H.;
RT "Structural studies on yeast 3-phosphoglycerate kinase. Linear arrangement
RT of the CNBr fragments, partial amino acid sequence of the inner part of the
RT polypeptide chain, and analyses of the N-terminal domain of the protein.";
RL Int. J. Pept. Protein Res. 17:393-400(1981).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 282-416.
RX PubMed=6347186; DOI=10.1042/bj2110199;
RA Perkins R.E., Conroy S.C., Dunbar B., Fothergill L.A., Tuite M.F.,
RA Dobson M.J., Kingsman S.M., Kingsman A.J.;
RT "The complete amino acid sequence of yeast phosphoglycerate kinase.";
RL Biochem. J. 211:199-218(1983).
RN [7]
RP PRELIMINARY PROTEIN SEQUENCE OF 268-398, AND NUCLEOTIDE SEQUENCE OF 2-7.
RX PubMed=6281737; DOI=10.1093/nar/10.8.2625;
RA Dobson M.J., Tuite M.F., Roberts N.A., Kingsman A.J., Kingsman S.M.,
RA Perkins R.E., Conroy S.C., Dunbar B., Fothergill L.A.;
RT "Conservation of high efficiency promoter sequences in Saccharomyces
RT cerevisiae.";
RL Nucleic Acids Res. 10:2625-2637(1982).
RN [8]
RP PROTEIN SEQUENCE OF 150-161; 198-209 AND 245-256.
RC STRAIN=ATCC 44827 / SKQ2N;
RX PubMed=9509572;
RX DOI=10.1002/(sici)1097-0061(199712)13:16<1519::aid-yea211>3.0.co;2-u;
RA Norbeck J., Blomberg A.;
RT "Two-dimensional electrophoretic separation of yeast proteins using a non-
RT linear wide range (pH 3-10) immobilized pH gradient in the first dimension;
RT reproducibility and evidence for isoelectric focusing of alkaline (pI > 7)
RT proteins.";
RL Yeast 13:1519-1534(1997).
RN [9]
RP MUTAGENESIS OF ARG-22.
RX PubMed=1628654; DOI=10.1111/j.1432-1033.1992.tb17016.x;
RA Walker P.A., Joao H.C., Littlechild J.A., Wiliams R.J.P., Watson H.C.;
RT "Characterisation of yeast phosphoglycerate kinase modified by mutagenesis
RT at residue 21.";
RL Eur. J. Biochem. 207:29-37(1992).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; THR-331 AND THR-392, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93; THR-203; THR-241 AND
RP THR-331, AND 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-172; THR-298;
RP SER-318; THR-331 AND THR-392, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-82; LYS-197; LYS-258; LYS-274
RP AND LYS-302, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [20]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ATP
RP ANALOG.
RX PubMed=6765200; DOI=10.1002/j.1460-2075.1982.tb01366.x;
RA Watson H.C., Walker N.P.C., Shaw P.J., Bryant T.N., Wendell P.L.,
RA Fothergill L.A., Perkins R.E., Conroy S.C., Dobson M.J., Tuite M.F.,
RA Kingsman A.J., Kingsman S.M.;
RT "Sequence and structure of yeast phosphoglycerate kinase.";
RL EMBO J. 1:1635-1640(1982).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT GLN-66 IN COMPLEX WITH
RP SUBSTRATE AND ATP ANALOG.
RX PubMed=8672447; DOI=10.1021/bi952500o;
RA McPhillips T.M., Hsu B.T., Sherman M.A., Mas M.T., Rees D.C.;
RT "Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed
RT with Mg-AMP-PNP and 3-phospho-D-glycerate.";
RL Biochemistry 35:4118-4127(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:6765200,
CC ECO:0000269|PubMed:8672447}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}.
CC Mitochondrion {ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 314000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; J01342; AAA88729.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42329.2; -; Genomic_DNA.
DR EMBL; M14438; AAA34864.1; -; Genomic_DNA.
DR EMBL; K00553; AAA34863.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006937; DAA07490.1; -; Genomic_DNA.
DR PIR; S19422; KIBYG.
DR RefSeq; NP_009938.2; NM_001178725.1.
DR PDB; 1FW8; X-ray; 2.30 A; A=74-416.
DR PDB; 1QPG; X-ray; 2.40 A; A=2-416.
DR PDB; 3PGK; X-ray; 2.50 A; A=2-416.
DR PDBsum; 1FW8; -.
DR PDBsum; 1QPG; -.
DR PDBsum; 3PGK; -.
DR AlphaFoldDB; P00560; -.
DR BMRB; P00560; -.
DR PCDDB; P00560; -.
DR SMR; P00560; -.
DR BioGRID; 30991; 141.
DR DIP; DIP-4152N; -.
DR IntAct; P00560; 50.
DR MINT; P00560; -.
DR STRING; 4932.YCR012W; -.
DR BindingDB; P00560; -.
DR ChEMBL; CHEMBL2674; -.
DR CarbonylDB; P00560; -.
DR iPTMnet; P00560; -.
DR COMPLUYEAST-2DPAGE; P00560; -.
DR MaxQB; P00560; -.
DR PaxDb; P00560; -.
DR PRIDE; P00560; -.
DR TopDownProteomics; P00560; -.
DR EnsemblFungi; YCR012W_mRNA; YCR012W; YCR012W.
DR GeneID; 850370; -.
DR KEGG; sce:YCR012W; -.
DR SGD; S000000605; PGK1.
DR VEuPathDB; FungiDB:YCR012W; -.
DR eggNOG; KOG1367; Eukaryota.
DR GeneTree; ENSGT00390000008820; -.
DR HOGENOM; CLU_025427_0_2_1; -.
DR InParanoid; P00560; -.
DR OMA; DMIFDIG; -.
DR BioCyc; YEAST:YCR012W-MON; -.
DR BRENDA; 2.7.2.3; 984.
DR Reactome; R-SCE-70171; Glycolysis.
DR Reactome; R-SCE-70263; Gluconeogenesis.
DR SABIO-RK; P00560; -.
DR UniPathway; UPA00109; UER00185.
DR EvolutionaryTrace; P00560; -.
DR PRO; PR:P00560; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P00560; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IDA:SGD.
DR GO; GO:0006094; P:gluconeogenesis; IMP:SGD.
DR GO; GO:0006096; P:glycolytic process; IMP:SGD.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 3.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Glycolysis; Isopeptide bond; Kinase;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..416
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145893"
FT BINDING 24..26
FT /ligand="substrate"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:6765200,
FT ECO:0000269|PubMed:8672447"
FT BINDING 63..66
FT /ligand="substrate"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:6765200,
FT ECO:0000269|PubMed:8672447"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:6765200,
FT ECO:0000269|PubMed:8672447"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 371..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 93
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 392
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 22
FT /note="R->K: 2-fold reduction of Vmax."
FT /evidence="ECO:0000269|PubMed:1628654"
FT MUTAGEN 22
FT /note="R->M: 7-fold reduction of Vmax."
FT /evidence="ECO:0000269|PubMed:1628654"
FT CONFLICT 185
FT /note="G -> S (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="E -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1QPG"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:1QPG"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:1QPG"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:1QPG"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1QPG"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3PGK"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1QPG"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3PGK"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1FW8"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:1FW8"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:3PGK"
FT HELIX 258..273
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 282..291
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:1FW8"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:3PGK"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 348..362
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 373..380
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:1FW8"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 395..401
FT /evidence="ECO:0007829|PDB:1FW8"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:1FW8"
SQ SEQUENCE 416 AA; 44738 MW; 378AB944DB34EFF0 CRC64;
MSLSSKLSVQ DLDLKDKRVF IRVDFNVPLD GKKITSNQRI VAALPTIKYV LEHHPRYVVL
ASHLGRPNGE RNEKYSLAPV AKELQSLLGK DVTFLNDCVG PEVEAAVKAS APGSVILLEN
LRYHIEEEGS RKVDGQKVKA SKEDVQKFRH ELSSLADVYI NDAFGTAHRA HSSMVGFDLP
QRAAGFLLEK ELKYFGKALE NPTRPFLAIL GGAKVADKIQ LIDNLLDKVD SIIIGGGMAF
TFKKVLENTE IGDSIFDKAG AEIVPKLMEK AKAKGVEVVL PVDFIIADAF SADANTKTVT
DKEGIPAGWQ GLDNGPESRK LFAATVAKAK TIVWNGPPGV FEFEKFAAGT KALLDEVVKS
SAAGNTVIIG GGDTATVAKK YGVTDKISHV STGGGASLEL LEGKELPGVA FLSEKK
