PROB_YEAST
ID PROB_YEAST Reviewed; 428 AA.
AC P32264; D6VSS9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Glutamate 5-kinase;
DE Short=GK;
DE EC=2.7.2.11;
DE AltName: Full=Gamma-glutamyl kinase;
GN Name=PRO1; OrderedLocusNames=YDR300C; ORFNames=D9740.12;
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=1350780; DOI=10.1128/jb.174.12.4148-4156.1992;
RA Li W., Brandriss M.C.;
RT "Proline biosynthesis in Saccharomyces cerevisiae: molecular analysis of
RT the PRO1 gene, which encodes gamma-glutamyl kinase.";
RL J. Bacteriol. 174:4148-4156(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 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).
CC -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to
CC form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate;
CC Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11;
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 1/2.
CC -!- INTERACTION:
CC P32264; P02829: HSP82; NbExp=3; IntAct=EBI-13879, EBI-8659;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 10400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family. {ECO:0000305}.
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DR EMBL; M85293; AAA34904.1; -; Genomic_DNA.
DR EMBL; U28374; AAB64736.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12139.1; -; Genomic_DNA.
DR PIR; S61186; S61186.
DR RefSeq; NP_010586.3; NM_001180608.3.
DR AlphaFoldDB; P32264; -.
DR SMR; P32264; -.
DR BioGRID; 32352; 34.
DR DIP; DIP-5221N; -.
DR IntAct; P32264; 12.
DR MINT; P32264; -.
DR STRING; 4932.YDR300C; -.
DR MaxQB; P32264; -.
DR PaxDb; P32264; -.
DR PRIDE; P32264; -.
DR TopDownProteomics; P32264; -.
DR EnsemblFungi; YDR300C_mRNA; YDR300C; YDR300C.
DR GeneID; 851894; -.
DR KEGG; sce:YDR300C; -.
DR SGD; S000002708; PRO1.
DR VEuPathDB; FungiDB:YDR300C; -.
DR eggNOG; KOG1154; Eukaryota.
DR GeneTree; ENSGT00500000044903; -.
DR HOGENOM; CLU_025400_1_1_1; -.
DR InParanoid; P32264; -.
DR OMA; TVIHRDN; -.
DR BioCyc; YEAST:YDR300C-MON; -.
DR BRENDA; 2.7.2.11; 984.
DR UniPathway; UPA00098; UER00359.
DR PRO; PR:P32264; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32264; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004349; F:glutamate 5-kinase activity; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006561; P:proline biosynthetic process; IDA:SGD.
DR GO; GO:0034517; P:ribophagy; IMP:SGD.
DR CDD; cd04242; AAK_G5K_ProB; 1.
DR Gene3D; 2.30.130.10; -; 1.
DR Gene3D; 3.40.1160.10; -; 2.
DR HAMAP; MF_00456; ProB; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR041739; G5K_ProB.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
DR InterPro; IPR011529; Glu_5kinase.
DR InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR InterPro; IPR019797; Glutamate_5-kinase_CS.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF01472; PUA; 1.
DR PIRSF; PIRSF000729; GK; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR01027; proB; 1.
DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR PROSITE; PS50890; PUA; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Proline biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..428
FT /note="Glutamate 5-kinase"
FT /id="PRO_0000109768"
FT DOMAIN 321..412
FT /note="PUA"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 175..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 219..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 332
FT /note="A -> R (in Ref. 1; AAA34904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 47162 MW; 0DBAC7CA98051C80 CRC64;
MKDANESKSY TIVIKLGSSS LVDEKTKEPK LAIMSLIVET VVKLRRMGHK VIIVSSGGIA
VGLRTMRMNK RPKHLAEVQA IAAIGQGRLI GRWDLLFSQF DQRIAQILLT RNDILDWTQY
KNAQNTINEL LNMGVIPIVN ENDTLSVREI KFGDNDTLSA ITSALIHADY LFLLTDVDCL
YTDNPRTNPD AMPILVVPDL SKGLPGVNTA GGSGSDVGTG GMETKLVAAD LATNAGVHTL
IMKSDTPANI GRIVEYMQTL ELDDENKVKQ AYNGDLTDLQ KREFEKLKAL NVPLHTKFIA
NDNKHHLKNR EFWILHGLVS KGAVVIDQGA YAALTRKNKA GLLPAGVIDV QGTFHELECV
DIKVGKKLPD GTLDPDFPLQ TVGKARCNYT SSELTKIKGL HSDQIEEELG YNDSEYVAHR
ENLAFPPR
