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A4W028

- PROA_STRS2

UniProt

A4W028 - PROA_STRS2

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Protein

Gamma-glutamyl phosphate reductase

Gene

proA

Organism
Streptococcus suis (strain 98HAH33)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.UniRule annotation

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. glutamate-5-semialdehyde dehydrogenase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciSSUI391296:GI2E-609-MONOMER.
UniPathwayiUPA00098; UER00360.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyl phosphate reductaseUniRule annotation (EC:1.2.1.41UniRule annotation)
Short name:
GPRUniRule annotation
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenaseUniRule annotation
Glutamyl-gamma-semialdehyde dehydrogenaseUniRule annotation
Short name:
GSA dehydrogenaseUniRule annotation
Gene namesi
Name:proAUniRule annotation
Ordered Locus Names:SSU98_0559
OrganismiStreptococcus suis (strain 98HAH33)
Taxonomic identifieri391296 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000000244: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412Gamma-glutamyl phosphate reductasePRO_1000049997Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi391296.SSU98_0559.

Structurei

3D structure databases

ProteinModelPortaliA4W028.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the gamma-glutamyl phosphate reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0014.
HOGENOMiHOG000246356.
KOiK00147.
OMAiALTSYKW.
OrthoDBiEOG6FFSCX.

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.
IPR000965. G-glutamylP_reductase.
IPR020593. G-glutamylP_reductase_CS.
IPR012134. Glu-5-SA_DH.
[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.

A4W028-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTTQVLLDS LLANKASINL ATTEQKNQAL SAMADQLVAQ TEAILAGNAI
60 70 80 90 100
DMEHAQGKIS QVMQDRLLLT EERIEAMADG IRALIGLPDP VGLVLEESTR
110 120 130 140 150
ADGLNICKKS IPFGLVGMIY ESRPNVTSDA AALAIKSGNA VILRGGKEAF
160 170 180 190 200
HSAKAIVTAL KSGLEEAGVS PKVIELVQDT SRVSATELMT AKGKIDLLVP
210 220 230 240 250
RGGAGLIQAV VENATVPVIE TGTGICHVYV DKDADLDKAL RIVVNAKTSR
260 270 280 290 300
PSVCNAAEVL LVHEEIASQF LPRLEEALSG QVELRADSQA QALLNQARPA
310 320 330 340 350
GDQDFDTEFL DYIMAVKVVS SVEEAISHIA QHSTGHSEAI VTENSQTAEH
360 370 380 390 400
FTLHVDSAAV YVNASTRFTD GGEFGLGCEL GISTQKMHAR GPMGLREMTT
410
YKYIITGDGH IR
Length:412
Mass (Da):43,863
Last modified:May 29, 2007 - v1
Checksum:iC688B33D7A3CFB64
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000408 Genomic DNA. Translation: ABP91717.1.
RefSeqiYP_001200117.1. NC_009443.1.

Genome annotation databases

EnsemblBacteriaiABP91717; ABP91717; SSU98_0559.
GeneIDi5103016.
KEGGissv:SSU98_0559.
PATRICi19777351. VBIStrSui72275_0545.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000408 Genomic DNA. Translation: ABP91717.1 .
RefSeqi YP_001200117.1. NC_009443.1.

3D structure databases

ProteinModelPortali A4W028.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 391296.SSU98_0559.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP91717 ; ABP91717 ; SSU98_0559 .
GeneIDi 5103016.
KEGGi ssv:SSU98_0559.
PATRICi 19777351. VBIStrSui72275_0545.

Phylogenomic databases

eggNOGi COG0014.
HOGENOMi HOG000246356.
KOi K00147.
OMAi ALTSYKW.
OrthoDBi EOG6FFSCX.

Enzyme and pathway databases

UniPathwayi UPA00098 ; UER00360 .
BioCyci SSUI391296:GI2E-609-MONOMER.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPi MF_00412. ProA.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR000965. G-glutamylP_reductase.
IPR020593. G-glutamylP_reductase_CS.
IPR012134. Glu-5-SA_DH.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000151. GPR. 1 hit.
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR00407. proA. 1 hit.
PROSITEi PS01223. PROA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A glimpse of streptococcal toxic shock syndrome from comparative genomics of S. suis 2 Chinese isolates."
    Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J., Dong Y.
    , Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F., Yang R., Wang J., Yu J.
    PLoS ONE 2:E315-E315(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 98HAH33.

Entry informationi

Entry nameiPROA_STRS2
AccessioniPrimary (citable) accession number: A4W028
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: October 29, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3