ID   KGUA_YEAST              Reviewed;         187 AA.
AC   P15454; D6VT79;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 217.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8 {ECO:0000269|PubMed:1334480};
DE   AltName: Full=GMP kinase;
GN   Name=GUK1; OrderedLocusNames=YDR454C; ORFNames=D9461.39;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=1334480; DOI=10.1016/s0021-9258(18)35654-0;
RA   Konrad M.;
RT   "Cloning and expression of the essential gene for guanylate kinase from
RT   yeast.";
RL   J. Biol. Chem. 267:25652-25655(1992).
RN   [2]
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   [3]
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   [4]
RP   PROTEIN SEQUENCE OF 2-187, CLEAVAGE OF INITIATOR METHIONINE, AND
RP   ACETYLATION AT SER-2.
RX   PubMed=2551688; DOI=10.1111/j.1432-1033.1989.tb15035.x;
RA   Berger A., Schiltz E., Schulz G.E.;
RT   "Guanylate kinase from Saccharomyces cerevisiae. Isolation and
RT   characterization, crystallization and preliminary X-ray analysis, amino
RT   acid sequence and comparison with adenylate kinases.";
RL   Eur. J. Biochem. 184:433-443(1989).
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP   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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND TYR-157, AND
RP   IDENTIFICATION BY 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   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=1967656; DOI=10.1016/0022-2836(90)90024-g;
RA   Stehle T., Schulz G.E.;
RT   "Three-dimensional structure of the complex of guanylate kinase from yeast
RT   with its substrate GMP.";
RL   J. Mol. Biol. 211:249-254(1990).
RN   [11] {ECO:0007744|PDB:1GKY}
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-187 IN COMPLEX WITH GMP.
RX   PubMed=1314905; DOI=10.1016/0022-2836(92)90474-x;
RA   Stehle T., Schulz G.E.;
RT   "Refined structure of the complex between guanylate kinase and its
RT   substrate GMP at 2.0-A resolution.";
RL   J. Mol. Biol. 224:1127-1141(1992).
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphoryl
CC       group of ATP to the acceptor molecule GMP. Essential for recycling GMP
CC       and indirectly, cGMP. {ECO:0000305|PubMed:1334480}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:456216; EC=2.7.4.8;
CC         Evidence={ECO:0000269|PubMed:1334480};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20781;
CC         Evidence={ECO:0000305|PubMed:1334480};
CC   -!- SUBUNIT: Monomer.
CC   -!- MISCELLANEOUS: Present with 20500 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
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DR   EMBL; L04683; AAA34657.1; -; Genomic_DNA.
DR   EMBL; U33007; AAB64881.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12289.1; -; Genomic_DNA.
DR   PIR; A45097; KIBYGU.
DR   RefSeq; NP_010742.1; NM_001180762.1.
DR   PDB; 1EX6; X-ray; 2.30 A; A/B=2-187.
DR   PDB; 1EX7; X-ray; 1.90 A; A=2-187.
DR   PDB; 1GKY; X-ray; 2.00 A; A=2-187.
DR   PDB; 4F4J; X-ray; 2.45 A; A/B=1-187.
DR   PDBsum; 1EX6; -.
DR   PDBsum; 1EX7; -.
DR   PDBsum; 1GKY; -.
DR   PDBsum; 4F4J; -.
DR   AlphaFoldDB; P15454; -.
DR   SMR; P15454; -.
DR   BioGRID; 32509; 198.
DR   DIP; DIP-6721N; -.
DR   IntAct; P15454; 2.
DR   MINT; P15454; -.
DR   STRING; 4932.YDR454C; -.
DR   iPTMnet; P15454; -.
DR   MaxQB; P15454; -.
DR   PaxDb; 4932-YDR454C; -.
DR   PeptideAtlas; P15454; -.
DR   TopDownProteomics; P15454; -.
DR   EnsemblFungi; YDR454C_mRNA; YDR454C; YDR454C.
DR   GeneID; 852065; -.
DR   KEGG; sce:YDR454C; -.
DR   AGR; SGD:S000002862; -.
DR   SGD; S000002862; GUK1.
DR   VEuPathDB; FungiDB:YDR454C; -.
DR   eggNOG; KOG0707; Eukaryota.
DR   GeneTree; ENSGT00940000155815; -.
DR   HOGENOM; CLU_001715_0_4_1; -.
DR   InParanoid; P15454; -.
DR   OMA; EWAVVHG; -.
DR   OrthoDB; 324675at2759; -.
DR   BioCyc; MetaCyc:MONOMER3O-102; -.
DR   BioCyc; YEAST:MONOMER3O-102; -.
DR   BRENDA; 2.7.4.8; 984.
DR   Reactome; R-SCE-499943; Interconversion of nucleotide di- and triphosphates.
DR   Reactome; R-SCE-9748787; Azathioprine ADME.
DR   BioGRID-ORCS; 852065; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P15454; -.
DR   PRO; PR:P15454; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P15454; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004385; F:guanylate kinase activity; IDA:SGD.
DR   GO; GO:0046711; P:GDP biosynthetic process; IMP:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; ISS:UniProtKB.
DR   CDD; cd00071; GMPK; 1.
DR   Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00328; Guanylate_kinase; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR017665; Guanylate_kinase.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03263; guanyl_kin; 1.
DR   PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1.
DR   PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2551688"
FT   CHAIN           2..187
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170655"
FT   DOMAIN          2..184
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT   BINDING         35
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000269|PubMed:1314905,
FT                   ECO:0000269|PubMed:1967656, ECO:0007744|PDB:1GKY"
FT   BINDING         39..42
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000269|PubMed:1314905,
FT                   ECO:0000269|PubMed:1967656, ECO:0007744|PDB:1GKY"
FT   BINDING         51
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000269|PubMed:1314905,
FT                   ECO:0000269|PubMed:1967656, ECO:0007744|PDB:1GKY"
FT   BINDING         70
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000269|PubMed:1314905,
FT                   ECO:0000269|PubMed:1967656, ECO:0007744|PDB:1GKY"
FT   BINDING         79..81
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000269|PubMed:1314905,
FT                   ECO:0000269|PubMed:1967656, ECO:0007744|PDB:1GKY"
FT   BINDING         101
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000269|PubMed:1314905,
FT                   ECO:0000269|PubMed:1967656, ECO:0007744|PDB:1GKY"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:1314905,
FT                   ECO:0000269|PubMed:2551688"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         157
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   STRAND          5..8
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   HELIX           15..25
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:1GKY"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:1GKY"
FT   HELIX           56..64
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   STRAND          68..74
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   STRAND          77..82
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   HELIX           83..92
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   STRAND          94..99
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   HELIX           102..109
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   STRAND          117..122
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   HELIX           126..136
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   HELIX           141..158
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   TURN            159..161
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   STRAND          163..168
FT                   /evidence="ECO:0007829|PDB:1EX7"
FT   HELIX           172..183
FT                   /evidence="ECO:0007829|PDB:1EX7"
SQ   SEQUENCE   187 AA;  20637 MW;  5DC4D2A22594BFB8 CRC64;
     MSRPIVISGP SGTGKSTLLK KLFAEYPDSF GFSVSSTTRT PRAGEVNGKD YNFVSVDEFK
     SMIKNNEFIE WAQFSGNYYG STVASVKQVS KSGKTCILDI DMQGVKSVKA IPELNARFLF
     IAPPSVEDLK KRLEGRGTET EESINKRLSA AQAELAYAET GAHDKVIVND DLDKAYKELK
     DFIFAEK
//