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P32264

- PROB_YEAST

UniProt

P32264 - PROB_YEAST

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Protein

Glutamate 5-kinase

Gene

PRO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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.

Pathwayi

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

  1. ATP binding Source: UniProtKB-KW
  2. glutamate 5-kinase activity Source: SGD
  3. identical protein binding Source: IntAct
  4. RNA binding Source: InterPro

GO - Biological processi

  1. L-proline biosynthetic process Source: UniProtKB-UniPathway
  2. 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: Chromosome IV

Organism-specific databases

CYGDiYDR300c.
SGDiS000002708. PRO1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
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.

Expressioni

Gene expression databases

GenevestigatoriP32264.

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.
OMAiPRIENAR.
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.
IPR011529. Glu_5kinase.
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]
PIRSFiPIRSF000729. GK. 1 hit.
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 .
PIRi S61186.
RefSeqi NP_010586.3. NM_001180608.3.

3D structure databases

ProteinModelPortali P32264.
SMRi P32264. Positions 9-423.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32352. 29 interactions.
DIPi DIP-5221N.
IntActi P32264. 10 interactions.
MINTi MINT-516807.
STRINGi 4932.YDR300C.

Proteomic databases

MaxQBi P32264.
PaxDbi P32264.
PeptideAtlasi P32264.
PRIDEi P32264.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR300C ; YDR300C ; YDR300C .
GeneIDi 851894.
KEGGi sce:YDR300C.

Organism-specific databases

CYGDi YDR300c.
SGDi S000002708. PRO1.

Phylogenomic databases

eggNOGi COG0263.
GeneTreei ENSGT00550000075661.
HOGENOMi HOG000246369.
InParanoidi P32264.
KOi K00931.
OMAi PRIENAR.
OrthoDBi EOG7SFJ62.

Enzyme and pathway databases

UniPathwayi UPA00098 ; UER00359 .
BioCyci YEAST:YDR300C-MONOMER.
BRENDAi 2.7.2.11. 984.

Miscellaneous databases

NextBioi 969886.

Gene expression databases

Genevestigatori P32264.

Family and domain databases

Gene3Di 2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPi MF_00456. ProB.
InterProi IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
IPR011529. Glu_5kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR002478. PUA.
IPR015947. PUA-like_domain.
[Graphical view ]
Pfami PF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view ]
PIRSFi PIRSF000729. GK. 1 hit.
PRINTSi PR00474. GLU5KINASE.
SMARTi SM00359. PUA. 1 hit.
[Graphical view ]
SUPFAMi SSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsi TIGR01027. proB. 1 hit.
PROSITEi PS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 131 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