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Protein

Gamma-glutamyl phosphate reductase

Gene

PRO2

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 NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.

Catalytic activityi

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.

Pathwayi: L-proline biosynthesis

This protein is involved in step 2 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.

GO - Molecular functioni

  • glutamate-5-semialdehyde dehydrogenase activity Source: SGD
  • NADP binding Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciYEAST:YOR323C-MONOMER.
ReactomeiR-SCE-70614. Amino acid synthesis and interconversion (transamination).
UniPathwayiUPA00098; UER00360.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyl phosphate reductase (EC:1.2.1.41)
Short name:
GPR
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase
Short name:
GSA dehydrogenase
Glutamyl-gamma-semialdehyde dehydrogenase
Gene namesi
Name:PRO2
Ordered Locus Names:YOR323C
ORF Names:O6155
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR323C.
SGDiS000005850. PRO2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 456455Gamma-glutamyl phosphate reductasePRO_0000189824Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP54885.
PeptideAtlasiP54885.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PTC6P256469EBI-13872,EBI-21989

Protein-protein interaction databases

BioGridi34709. 30 interactions.
DIPiDIP-6586N.
IntActiP54885. 10 interactions.
MINTiMINT-615046.

Structurei

Secondary structure

1
456
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1816Combined sources
Helixi23 – 3917Combined sources
Helixi41 – 5717Combined sources
Helixi62 – 687Combined sources
Helixi75 – 8814Combined sources
Beta strandi92 – 943Combined sources
Beta strandi96 – 1038Combined sources
Beta strandi106 – 1149Combined sources
Beta strandi117 – 1248Combined sources
Helixi127 – 13913Combined sources
Beta strandi142 – 1465Combined sources
Helixi149 – 1513Combined sources
Helixi152 – 17322Combined sources
Beta strandi179 – 1824Combined sources
Helixi190 – 1945Combined sources
Turni196 – 1983Combined sources
Beta strandi201 – 2066Combined sources
Helixi208 – 2169Combined sources
Beta strandi230 – 2345Combined sources
Helixi240 – 24910Combined sources
Beta strandi262 – 2665Combined sources
Helixi273 – 28412Combined sources
Beta strandi288 – 2903Combined sources
Helixi292 – 30514Combined sources
Helixi310 – 3134Combined sources
Beta strandi335 – 3384Combined sources
Helixi342 – 3498Combined sources
Beta strandi357 – 3615Combined sources
Helixi365 – 37410Combined sources
Beta strandi378 – 3847Combined sources
Helixi386 – 3883Combined sources
Helixi416 – 4183Combined sources
Beta strandi419 – 4268Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VLUX-ray2.29A/B1-456[»]
ProteinModelPortaliP54885.
SMRiP54885. Positions 1-435.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54885.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00500000044903.
HOGENOMiHOG000246356.
InParanoidiP54885.
KOiK00147.
OMAiCNAIETL.
OrthoDBiEOG7DVDN4.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPiMF_00412. ProA.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR020593. G-glutamylP_reductase_CS.
IPR012134. Glu-5-SA_DH.
IPR000965. GPR_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF000151. GPR. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00407. proA. 1 hit.
PROSITEiPS01223. PROA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54885-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSQQIAKN ARKAGNILKT ISNEGRSDIL YKIHDALKAN AHAIEEANKI
60 70 80 90 100
DLAVAKETGL ADSLLKRLDL FKGDKFEVML QGIKDVAELE DPVGKVKMAR
110 120 130 140 150
ELDDGLTLYQ VTAPVGVLLV IFESRPEVIA NITALSIKSG NAAILKGGKE
160 170 180 190 200
SVNTFREMAK IVNDTIAQFQ SETGVPVGSV QLIETRQDVS DLLDQDEYID
210 220 230 240 250
LVVPRGSNAL VRKIKDTTKI PVLGHADGIC SIYLDEDADL IKAKRISLDA
260 270 280 290 300
KTNYPAGCNA METLLINPKF SKWWEVLENL TLEGGVTIHA TKDLKTAYFD
310 320 330 340 350
KLNELGKLTE AIQCKTVDAD EEQDFDKEFL SLDLAAKFVT STESAIQHIN
360 370 380 390 400
THSSRHTDAI VTENKANAEK FMKGVDSSGV YWNASTRFAD GFRYGFGAEV
410 420 430 440 450
GISTSKIHAR GPVGLDGLVS YQYQIRGDGQ VASDYLGAGG NKAFVHKDLD

IKTVTL
Length:456
Mass (Da):49,740
Last modified:October 1, 1996 - v1
Checksum:i7EDEC40C9B3DB07D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43565 Genomic DNA. Translation: AAA86261.1.
X90565 Genomic DNA. Translation: CAA62179.1.
Z75231 Genomic DNA. Translation: CAA99643.1.
AY692984 Genomic DNA. Translation: AAT93003.1.
BK006948 Genomic DNA. Translation: DAA11087.1.
PIRiS58334.
RefSeqiNP_014968.1. NM_001183743.1.

Genome annotation databases

EnsemblFungiiYOR323C; YOR323C; YOR323C.
GeneIDi854501.
KEGGisce:YOR323C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43565 Genomic DNA. Translation: AAA86261.1.
X90565 Genomic DNA. Translation: CAA62179.1.
Z75231 Genomic DNA. Translation: CAA99643.1.
AY692984 Genomic DNA. Translation: AAT93003.1.
BK006948 Genomic DNA. Translation: DAA11087.1.
PIRiS58334.
RefSeqiNP_014968.1. NM_001183743.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VLUX-ray2.29A/B1-456[»]
ProteinModelPortaliP54885.
SMRiP54885. Positions 1-435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34709. 30 interactions.
DIPiDIP-6586N.
IntActiP54885. 10 interactions.
MINTiMINT-615046.

Proteomic databases

MaxQBiP54885.
PeptideAtlasiP54885.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR323C; YOR323C; YOR323C.
GeneIDi854501.
KEGGisce:YOR323C.

Organism-specific databases

EuPathDBiFungiDB:YOR323C.
SGDiS000005850. PRO2.

Phylogenomic databases

GeneTreeiENSGT00500000044903.
HOGENOMiHOG000246356.
InParanoidiP54885.
KOiK00147.
OMAiCNAIETL.
OrthoDBiEOG7DVDN4.

Enzyme and pathway databases

UniPathwayiUPA00098; UER00360.
BioCyciYEAST:YOR323C-MONOMER.
ReactomeiR-SCE-70614. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

EvolutionaryTraceiP54885.
PROiP54885.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPiMF_00412. ProA.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR020593. G-glutamylP_reductase_CS.
IPR012134. Glu-5-SA_DH.
IPR000965. GPR_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF000151. GPR. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00407. proA. 1 hit.
PROSITEiPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in Saccharomyces cerevisiae CTD kinase gene CTK1 are synthetic lethals with mutant versions of SSD1 and PRO2."
    Lee J.M., Greenleaf A.L.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII."
    Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A., Schweizer M.
    Yeast 12:1021-1031(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPROA_YEAST
AccessioniPrimary (citable) accession number: P54885
Secondary accession number(s): D6W321
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6920 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.