KAD2_YEAST
ID KAD2_YEAST Reviewed; 222 AA.
AC P07170; D6VSK8; Q6Q539;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_03168};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=Adenylate kinase cytosolic and mitochondrial {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03168};
DE Flags: Precursor;
GN Name=ADK1 {ECO:0000255|HAMAP-Rule:MF_03168}; Synonyms=AKY, AKY1, AKY2;
GN OrderedLocusNames=YDR226W; ORFNames=YD9934.11;
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=2834097; DOI=10.1007/bf00434817;
RA Magdolen V., Oechsner U., Bandlow W.;
RT "The complete nucleotide sequence of the gene coding for yeast adenylate
RT kinase.";
RL Curr. Genet. 12:405-411(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2821496; DOI=10.1093/nar/15.17.7187;
RA Proba K., Tomasselli A.G., Nielsen P., Schulz G.E.;
RT "The cDNA sequence encoding cytosolic adenylate kinase from baker's yeast
RT (Saccharomyces cerevisiae).";
RL Nucleic Acids Res. 15:7187-7187(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2848829; DOI=10.1016/s0021-9258(19)77657-1;
RA Konrad M.;
RT "Analysis and in vivo disruption of the gene coding for adenylate kinase
RT (ADK1) in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 263:19468-19474(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7885847; DOI=10.1093/nar/23.3.507;
RA Davies C.J., Hutchison C.A. III;
RT "Insertion site specificity of the transposon Tn3.";
RL Nucleic Acids Res. 23:507-514(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [8]
RP PROTEIN SEQUENCE OF 3-222, AND ACETYLATION AT SER-3.
RX PubMed=3004985; DOI=10.1111/j.1432-1033.1986.tb09465.x;
RA Tomasselli A.G., Mast E., Janes W., Schiltz E.;
RT "The complete amino acid sequence of adenylate kinase from baker's yeast.";
RL Eur. J. Biochem. 155:111-119(1986).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=2850178; DOI=10.1111/j.1432-1033.1988.tb14469.x;
RA Bandlow W., Strobel G., Zoglowek C., Oechsner U., Magdolen V.;
RT "Yeast adenylate kinase is active simultaneously in mitochondria and
RT cytoplasm and is required for non-fermentative growth.";
RL Eur. J. Biochem. 178:451-457(1988).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=12045196; DOI=10.1074/jbc.m201561200;
RA Schricker R., Angermayr M., Strobel G., Klinke S., Korber D., Bandlow W.;
RT "Redundant mitochondrial targeting signals in yeast adenylate kinase.";
RL J. Biol. Chem. 277:28757-28764(2002).
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 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 [13]
RP FUNCTION.
RX PubMed=18433446; DOI=10.1111/j.1365-2958.2008.06261.x;
RA Gauthier S., Coulpier F., Jourdren L., Merle M., Beck S., Konrad M.,
RA Daignan-Fornier B., Pinson B.;
RT "Co-regulation of yeast purine and phosphate pathways in response to
RT adenylic nucleotide variations.";
RL Mol. Microbiol. 68:1583-1594(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [15]
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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 3-221 IN COMPLEX WITH
RP BI-SUBSTRATE ANALOG AP5A.
RX PubMed=7635152; DOI=10.1111/j.1432-1033.1995.tb20713.x;
RA Spuergin P., Abele U., Schulz G.E.;
RT "Stability, activity and structure of adenylate kinase mutants.";
RL Eur. J. Biochem. 231:405-413(1995).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG
RP AP5A.
RX PubMed=7670369; DOI=10.1002/pro.5560040702;
RA Abele U., Schulz G.E.;
RT "High-resolution structures of adenylate kinase from yeast ligated with
RT inhibitor Ap5A, showing the pathway of phosphoryl transfer.";
RL Protein Sci. 4:1262-1271(1995).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 3-221 IN COMPLEX WITH ATP ANALOG.
RX PubMed=8594191; DOI=10.1006/jmbi.1996.0080;
RA Schlauderer G.J., Proba K., Schulz G.E.;
RT "Structure of a mutant adenylate kinase ligated with an ATP-analogue
RT showing domain closure over ATP.";
RL J. Mol. Biol. 256:223-227(1996).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Plays an important role in cellular energy
CC homeostasis and in adenine nucleotide metabolism. Adenylate kinase
CC activity is critical for regulation of the phosphate utilization and
CC the AMP de novo biosynthesis pathways. {ECO:0000255|HAMAP-
CC Rule:MF_03168, ECO:0000269|PubMed:18433446, ECO:0000269|PubMed:2848829,
CC ECO:0000269|PubMed:2850178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03168,
CC ECO:0000269|PubMed:2850178};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03168,
CC ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369,
CC ECO:0000269|PubMed:8594191}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-
CC Rule:MF_03168, ECO:0000269|PubMed:12045196,
CC ECO:0000269|PubMed:2850178}. Mitochondrion intermembrane space
CC {ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:12045196,
CC ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:22984289,
CC ECO:0000269|PubMed:2850178}. Note=90% cytoplasmic, 10% mitochondrial.
CC {ECO:0000269|PubMed:2850178}.
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC small peripheral domains, NMPbind and LID, which undergo movements
CC during catalysis. The LID domain closes over the site of phosphoryl
CC transfer upon ATP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent ATP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03168,
CC ECO:0000305|PubMed:24374639, ECO:0000305|PubMed:7635152,
CC ECO:0000305|PubMed:8594191}.
CC -!- DISRUPTION PHENOTYPE: The phenotype of disruption mutants is pet,
CC showing that complementation by another adenylate kinase isozyme occurs
CC only under fermentative conditions. The disruption completely destroys
CC the activity in mitochondria, whereas in the cytoplasmic fraction about
CC 10% is retained. {ECO:0000269|PubMed:2850178}.
CC -!- MISCELLANEOUS: Present with 123000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03168}.
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DR EMBL; X06304; CAA29624.1; -; Genomic_DNA.
DR EMBL; Y00413; CAA68471.1; -; mRNA.
DR EMBL; M18455; AAA66319.1; -; Genomic_DNA.
DR EMBL; U13239; AAC33143.1; -; Genomic_DNA.
DR EMBL; Z48612; CAA88506.1; -; Genomic_DNA.
DR EMBL; AY558578; AAS56904.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12068.1; -; Genomic_DNA.
DR PIR; S05799; KIBYA.
DR RefSeq; NP_010512.1; NM_001180534.1.
DR PDB; 1AKY; X-ray; 1.63 A; A=3-221.
DR PDB; 1DVR; X-ray; 2.36 A; A/B=3-221.
DR PDB; 2AKY; X-ray; 1.96 A; A=3-221.
DR PDB; 3AKY; X-ray; 2.23 A; A=3-221.
DR PDBsum; 1AKY; -.
DR PDBsum; 1DVR; -.
DR PDBsum; 2AKY; -.
DR PDBsum; 3AKY; -.
DR AlphaFoldDB; P07170; -.
DR SMR; P07170; -.
DR BioGRID; 32278; 96.
DR DIP; DIP-5129N; -.
DR IntAct; P07170; 12.
DR MINT; P07170; -.
DR STRING; 4932.YDR226W; -.
DR iPTMnet; P07170; -.
DR SWISS-2DPAGE; P07170; -.
DR MaxQB; P07170; -.
DR PaxDb; P07170; -.
DR PRIDE; P07170; -.
DR TopDownProteomics; P07170; -.
DR EnsemblFungi; YDR226W_mRNA; YDR226W; YDR226W.
DR GeneID; 851812; -.
DR KEGG; sce:YDR226W; -.
DR SGD; S000002634; ADK1.
DR VEuPathDB; FungiDB:YDR226W; -.
DR eggNOG; KOG3078; Eukaryota.
DR GeneTree; ENSGT00940000154576; -.
DR HOGENOM; CLU_032354_1_0_1; -.
DR InParanoid; P07170; -.
DR OMA; FHNRMRV; -.
DR BioCyc; MetaCyc:YDR226W-MON; -.
DR BioCyc; YEAST:YDR226W-MON; -.
DR Reactome; R-SCE-499943; Interconversion of nucleotide di- and triphosphates.
DR SABIO-RK; P07170; -.
DR EvolutionaryTrace; P07170; -.
DR PRO; PR:P07170; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P07170; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006172; P:ADP biosynthetic process; IDA:SGD.
DR GO; GO:0046033; P:AMP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR GO; GO:0009117; P:nucleotide metabolic process; IMP:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR HAMAP; MF_03168; Adenylate_kinase_AK2; 1.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR028587; AK2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT PROPEP 2
FT /note="Removed in mature form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:3004985"
FT /id="PRO_0000016550"
FT CHAIN 3..222
FT /note="Adenylate kinase"
FT /id="PRO_0000016551"
FT REGION 36..65
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369"
FT REGION 133..170
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369"
FT BINDING 16..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369,
FT ECO:0000269|PubMed:8594191"
FT BINDING 37
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369"
FT BINDING 42
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369"
FT BINDING 63..65
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369"
FT BINDING 92..95
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369"
FT BINDING 99
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369,
FT ECO:0000269|PubMed:8594191"
FT BINDING 143..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:7635152,
FT ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191"
FT BINDING 167
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369"
FT BINDING 178
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369,
FT ECO:0000269|PubMed:8594191"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="N-acetylserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:3004985"
FT CONFLICT 95
FT /note="R -> K (in Ref. 7; AAS56904)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="A -> R (in Ref. 2; CAA68471)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="D -> N (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:1AKY"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:1AKY"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1AKY"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1AKY"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:1AKY"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:1AKY"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1AKY"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:1AKY"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:1AKY"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:1AKY"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:1AKY"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1AKY"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1AKY"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1AKY"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1AKY"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:1AKY"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:1AKY"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:1AKY"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1AKY"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:1AKY"
SQ SEQUENCE 222 AA; 24255 MW; FE566FD8015907CE CRC64;
MSSSESIRMV LIGPPGAGKG TQAPNLQERF HAAHLATGDM LRSQIAKGTQ LGLEAKKIMD
QGGLVSDDIM VNMIKDELTN NPACKNGFIL DGFPRTIPQA EKLDQMLKEQ GTPLEKAIEL
KVDDELLVAR ITGRLIHPAS GRSYHKIFNP PKEDMKDDVT GEALVQRSDD NADALKKRLA
AYHAQTEPIV DFYKKTGIWA GVDASQPPAT VWADILNKLG KD
