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Protein

Gamma-glutamyl phosphate reductase

Gene

proA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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: L-proline biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamate 5-kinase (proB), Glutamate 5-kinase (proB)
  2. Gamma-glutamyl phosphate reductase (proA), Gamma-glutamyl phosphate reductase (proA)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.2.1.41. 6331.
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:TM_0293
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415Gamma-glutamyl phosphate reductasePRO_0000189802Add
BLAST

Proteomic databases

PRIDEiQ9WYC9.

Interactioni

Protein-protein interaction databases

STRINGi243274.TM0293.

Structurei

Secondary structure

1
415
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1816Combined sources
Helixi23 – 3917Combined sources
Helixi41 – 5717Combined sources
Helixi62 – 687Combined sources
Helixi72 – 8716Combined sources
Beta strandi95 – 1006Combined sources
Beta strandi106 – 1138Combined sources
Beta strandi117 – 1204Combined sources
Helixi126 – 13712Combined sources
Beta strandi142 – 1454Combined sources
Helixi148 – 1503Combined sources
Helixi151 – 16515Combined sources
Beta strandi168 – 1703Combined sources
Helixi172 – 1743Combined sources
Beta strandi175 – 1773Combined sources
Helixi184 – 1896Combined sources
Turni193 – 1953Combined sources
Beta strandi197 – 2015Combined sources
Helixi205 – 21410Combined sources
Beta strandi227 – 2315Combined sources
Helixi237 – 24913Combined sources
Beta strandi257 – 2648Combined sources
Helixi265 – 28117Combined sources
Beta strandi285 – 2884Combined sources
Helixi290 – 2956Combined sources
Beta strandi299 – 3013Combined sources
Helixi304 – 3063Combined sources
Beta strandi313 – 32311Combined sources
Helixi324 – 33411Combined sources
Beta strandi337 – 3437Combined sources
Helixi347 – 35610Combined sources
Beta strandi359 – 3668Combined sources
Helixi368 – 3703Combined sources
Turni373 – 3775Combined sources
Beta strandi387 – 3904Combined sources
Helixi398 – 4003Combined sources
Beta strandi401 – 4088Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O20X-ray2.00A1-415[»]
ProteinModelPortaliQ9WYC9.
SMRiQ9WYC9. Positions 2-415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WYC9.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C2S. Bacteria.
COG0014. LUCA.
InParanoidiQ9WYC9.
KOiK00147.
OMAiCNAIETL.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPiMF_00412. ProA. 1 hit.
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. 2 hits.
[Graphical view]
PIRSFiPIRSF000151. GPR. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00407. proA. 1 hit.
PROSITEiPS01223. PROA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WYC9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDELLEKAKK VREAWDVLRN ATTREKNKAI KKIAEKLDER RKEILEANRI
60 70 80 90 100
DVEKARERGV KESLVDRLAL NDKRIDEMIK ACETVIGLKD PVGEVIDSWV
110 120 130 140 150
REDGLRIARV RVPIGPIGII YESRPNVTVE TTILALKSGN TILLRGGSDA
160 170 180 190 200
LNSNKAIVSA IREALKETEI PESSVEFIEN TDRSLVLEMI RLREYLSLVI
210 220 230 240 250
PRGGYGLISF VRDNATVPVL ETGVGNCHIF VDESADLKKA VPVIINAKTQ
260 270 280 290 300
RPGTCNAAEK LLVHEKIAKE FLPVIVEELR KHGVEVRGCE KTREIVPDVV
310 320 330 340 350
PATEDDWPTE YLDLIIAIKV VKNVDEAIEH IKKYSTGHSE SILTENYSNA
360 370 380 390 400
KKFVSEIDAA AVYVNASTRF TDGGQFGFGA EIGISTQRFH ARGPVGLREL
410
TTYKFVVLGE YHVRE
Length:415
Mass (Da):46,404
Last modified:November 1, 1999 - v1
Checksum:i95BD703ACBE6F2AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35381.1.
PIRiE72394.
RefSeqiNP_228105.1. NC_000853.1.
WP_004083010.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35381; AAD35381; TM_0293.
GeneIDi897218.
KEGGitma:TM0293.
tmi:THEMA_03260.
tmw:THMA_0300.
PATRICi23935465. VBITheMar51294_0298.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35381.1.
PIRiE72394.
RefSeqiNP_228105.1. NC_000853.1.
WP_004083010.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O20X-ray2.00A1-415[»]
ProteinModelPortaliQ9WYC9.
SMRiQ9WYC9. Positions 2-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0293.

Proteomic databases

PRIDEiQ9WYC9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35381; AAD35381; TM_0293.
GeneIDi897218.
KEGGitma:TM0293.
tmi:THEMA_03260.
tmw:THMA_0300.
PATRICi23935465. VBITheMar51294_0298.

Phylogenomic databases

eggNOGiENOG4105C2S. Bacteria.
COG0014. LUCA.
InParanoidiQ9WYC9.
KOiK00147.
OMAiCNAIETL.

Enzyme and pathway databases

UniPathwayiUPA00098; UER00360.
BRENDAi1.2.1.41. 6331.

Miscellaneous databases

EvolutionaryTraceiQ9WYC9.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPiMF_00412. ProA. 1 hit.
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. 2 hits.
[Graphical view]
PIRSFiPIRSF000151. GPR. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00407. proA. 1 hit.
PROSITEiPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPROA_THEMA
AccessioniPrimary (citable) accession number: Q9WYC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1999
Last modified: September 7, 2016
This is version 129 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

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

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.