KGUA_YEAST
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 03-AUG-2022, entry version 211.
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; 194.
DR DIP; DIP-6721N; -.
DR IntAct; P15454; 2.
DR MINT; P15454; -.
DR STRING; 4932.YDR454C; -.
DR iPTMnet; P15454; -.
DR MaxQB; P15454; -.
DR PaxDb; P15454; -.
DR PRIDE; P15454; -.
DR TopDownProteomics; P15454; -.
DR EnsemblFungi; YDR454C_mRNA; YDR454C; YDR454C.
DR GeneID; 852065; -.
DR KEGG; sce:YDR454C; -.
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 BioCyc; MetaCyc:MON3O-102; -.
DR BioCyc; YEAST:MON3O-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 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 Gene3D; 3.40.50.300; -; 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 Pfam; PF00625; Guanylate_kin; 1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03263; guanyl_kin; 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
