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Q9RTD9

- PROA_DEIRA

UniProt

Q9RTD9 - PROA_DEIRA

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Protein

Gamma-glutamyl phosphate reductase

Gene

proA

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
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

BioCyciDRAD243230:GH46-1858-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:DR_1826
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002524: Chromosome I

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 – 432432Gamma-glutamyl phosphate reductasePRO_0000189720Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243230.DR_1826.

Structurei

3D structure databases

ProteinModelPortaliQ9RTD9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0014.
HOGENOMiHOG000246356.
InParanoidiQ9RTD9.
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.

Q9RTD9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTQTDSLPGV QATVQDMGER ARRAARVLRS LPTGRKVQAL RALAAELRAR
60 70 80 90 100
EAGILAANAQ DVQAAEAAGL PAPLVDRLRL SAGALAAIAR DVEAVAALPD
110 120 130 140 150
PVGEQTDEKT LPSGIRVSQR RVPLGVLGVI YESRPNVTVD VAALALMSGN
160 170 180 190 200
AAILRGGKET VNSNAALEDA IHAALNREGL PADAVQVIRD PDRARMLELL
210 220 230 240 250
RLDESVDAII PRGGAGLHRF CVENATVPVI VGGIGVVHIY LDGSFVQTPQ
260 270 280 290 300
DVQIAAALIR NAKTQKPSAC NALDTLLIDR AALAALPDVV RPLLESGVEV
310 320 330 340 350
RADAEAQAAL AGAGLNVTSA QLGDYGTEFL ALVASLRTVS GLDEALDFIA
360 370 380 390 400
ERGGHTDVIL TRDPAQAERF VQDVDSAAVM VNVSPRFNDG GQLGLGAEVA
410 420 430
ISTQKLHARG PMGLRELTTS KWVVRGEGQV RD
Length:432
Mass (Da):45,233
Last modified:May 1, 2000 - v1
Checksum:i913FF295EAEAD1DB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000513 Genomic DNA. Translation: AAF11380.1.
PIRiD75348.
RefSeqiNP_295549.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF11380; AAF11380; DR_1826.
GeneIDi1799066.
KEGGidra:DR_1826.
PATRICi21631288. VBIDeiRad64572_2038.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000513 Genomic DNA. Translation: AAF11380.1 .
PIRi D75348.
RefSeqi NP_295549.1. NC_001263.1.

3D structure databases

ProteinModelPortali Q9RTD9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243230.DR_1826.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF11380 ; AAF11380 ; DR_1826 .
GeneIDi 1799066.
KEGGi dra:DR_1826.
PATRICi 21631288. VBIDeiRad64572_2038.

Phylogenomic databases

eggNOGi COG0014.
HOGENOMi HOG000246356.
InParanoidi Q9RTD9.
KOi K00147.
OMAi ALTSYKW.
OrthoDBi EOG6FFSCX.

Enzyme and pathway databases

UniPathwayi UPA00098 ; UER00360 .
BioCyci DRAD243230:GH46-1858-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Entry informationi

Entry nameiPROA_DEIRA
AccessioniPrimary (citable) accession number: Q9RTD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 113 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, Reference proteome

Documents

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

External Data

Dasty 3