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Protein

Glutamate 5-kinase

Gene

PRO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline.

Catalytic activityi

ATP + L-glutamate = ADP + L-glutamate 5-phosphate.

Pathway: L-proline biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamate 5-kinase (PRO1)
  2. Gamma-glutamyl phosphate reductase (PRO2)
This subpathway is part of the pathway L-proline biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate, the pathway L-proline biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561SubstrateBy similarity
Binding sitei143 – 1431SubstrateBy similarity
Binding sitei155 – 1551Substrate; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi175 – 1762ATPBy similarity
Nucleotide bindingi219 – 2257ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • glutamate 5-kinase activity Source: SGD
  • identical protein binding Source: IntAct
  • RNA binding Source: InterPro

GO - Biological processi

  • L-proline biosynthetic process Source: UniProtKB-UniPathway
  • proline biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YDR300C-MONOMER.
BRENDAi2.7.2.11. 984.
UniPathwayiUPA00098; UER00359.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate 5-kinase (EC:2.7.2.11)
Short name:
GK
Alternative name(s):
Gamma-glutamyl kinase
Gene namesi
Name:PRO1
Ordered Locus Names:YDR300C
ORF Names:D9740.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR300c.
EuPathDBiFungiDB:YDR300C.
SGDiS000002708. PRO1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Glutamate 5-kinasePRO_0000109768Add
BLAST

Proteomic databases

MaxQBiP32264.
PaxDbiP32264.
PeptideAtlasiP32264.
PRIDEiP32264.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-13879,EBI-13879
HSP82P028293EBI-13879,EBI-8659

Protein-protein interaction databases

BioGridi32352. 29 interactions.
DIPiDIP-5221N.
IntActiP32264. 10 interactions.
MINTiMINT-516807.
STRINGi4932.YDR300C.

Structurei

3D structure databases

ProteinModelPortaliP32264.
SMRiP32264. Positions 9-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini321 – 41292PUAAdd
BLAST

Sequence similaritiesi

Belongs to the glutamate 5-kinase family.Curated
Contains 1 PUA domain.Curated

Phylogenomic databases

eggNOGiCOG0263.
GeneTreeiENSGT00550000075661.
HOGENOMiHOG000246369.
InParanoidiP32264.
KOiK00931.
OMAiGMSTKII.
OrthoDBiEOG7SFJ62.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPiMF_00456. ProB.
InterProiIPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR002478. PUA.
IPR015947. PUA-like_domain.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PRINTSiPR00474. GLU5KINASE.
SMARTiSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR01027. proB. 1 hit.
PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32264-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDANESKSY TIVIKLGSSS LVDEKTKEPK LAIMSLIVET VVKLRRMGHK
60 70 80 90 100
VIIVSSGGIA VGLRTMRMNK RPKHLAEVQA IAAIGQGRLI GRWDLLFSQF
110 120 130 140 150
DQRIAQILLT RNDILDWTQY KNAQNTINEL LNMGVIPIVN ENDTLSVREI
160 170 180 190 200
KFGDNDTLSA ITSALIHADY LFLLTDVDCL YTDNPRTNPD AMPILVVPDL
210 220 230 240 250
SKGLPGVNTA GGSGSDVGTG GMETKLVAAD LATNAGVHTL IMKSDTPANI
260 270 280 290 300
GRIVEYMQTL ELDDENKVKQ AYNGDLTDLQ KREFEKLKAL NVPLHTKFIA
310 320 330 340 350
NDNKHHLKNR EFWILHGLVS KGAVVIDQGA YAALTRKNKA GLLPAGVIDV
360 370 380 390 400
QGTFHELECV DIKVGKKLPD GTLDPDFPLQ TVGKARCNYT SSELTKIKGL
410 420
HSDQIEEELG YNDSEYVAHR ENLAFPPR
Length:428
Mass (Da):47,162
Last modified:October 1, 1996 - v2
Checksum:i0DBAC7CA98051C80
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti332 – 3321A → R in AAA34904 (PubMed:1350780).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85293 Genomic DNA. Translation: AAA34904.1.
U28374 Genomic DNA. Translation: AAB64736.1.
BK006938 Genomic DNA. Translation: DAA12139.1.
PIRiS61186.
RefSeqiNP_010586.3. NM_001180608.3.

Genome annotation databases

EnsemblFungiiYDR300C; YDR300C; YDR300C.
GeneIDi851894.
KEGGisce:YDR300C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85293 Genomic DNA. Translation: AAA34904.1.
U28374 Genomic DNA. Translation: AAB64736.1.
BK006938 Genomic DNA. Translation: DAA12139.1.
PIRiS61186.
RefSeqiNP_010586.3. NM_001180608.3.

3D structure databases

ProteinModelPortaliP32264.
SMRiP32264. Positions 9-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32352. 29 interactions.
DIPiDIP-5221N.
IntActiP32264. 10 interactions.
MINTiMINT-516807.
STRINGi4932.YDR300C.

Proteomic databases

MaxQBiP32264.
PaxDbiP32264.
PeptideAtlasiP32264.
PRIDEiP32264.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR300C; YDR300C; YDR300C.
GeneIDi851894.
KEGGisce:YDR300C.

Organism-specific databases

CYGDiYDR300c.
EuPathDBiFungiDB:YDR300C.
SGDiS000002708. PRO1.

Phylogenomic databases

eggNOGiCOG0263.
GeneTreeiENSGT00550000075661.
HOGENOMiHOG000246369.
InParanoidiP32264.
KOiK00931.
OMAiGMSTKII.
OrthoDBiEOG7SFJ62.

Enzyme and pathway databases

UniPathwayiUPA00098; UER00359.
BioCyciYEAST:YDR300C-MONOMER.
BRENDAi2.7.2.11. 984.

Miscellaneous databases

NextBioi969886.
PROiP32264.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPiMF_00456. ProB.
InterProiIPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR002478. PUA.
IPR015947. PUA-like_domain.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PRINTSiPR00474. GLU5KINASE.
SMARTiSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR01027. proB. 1 hit.
PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Proline biosynthesis in Saccharomyces cerevisiae: molecular analysis of the PRO1 gene, which encodes gamma-glutamyl kinase."
    Li W., Brandriss M.C.
    J. Bacteriol. 174:4148-4156(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPROB_YEAST
AccessioniPrimary (citable) accession number: P32264
Secondary accession number(s): D6VSS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 10400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.