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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)DescriptionActionsGraphical viewLength
ChainiPRO_00001898021 – 415Gamma-glutamyl phosphate reductaseAdd BLAST415

Proteomic databases

PRIDEiQ9WYC9.

Interactioni

Protein-protein interaction databases

STRINGi243274.TM0293.

Structurei

Secondary structure

1415
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 18Combined sources16
Helixi23 – 39Combined sources17
Helixi41 – 57Combined sources17
Helixi62 – 68Combined sources7
Helixi72 – 87Combined sources16
Beta strandi95 – 100Combined sources6
Beta strandi106 – 113Combined sources8
Beta strandi117 – 120Combined sources4
Helixi126 – 137Combined sources12
Beta strandi142 – 145Combined sources4
Helixi148 – 150Combined sources3
Helixi151 – 165Combined sources15
Beta strandi168 – 170Combined sources3
Helixi172 – 174Combined sources3
Beta strandi175 – 177Combined sources3
Helixi184 – 189Combined sources6
Turni193 – 195Combined sources3
Beta strandi197 – 201Combined sources5
Helixi205 – 214Combined sources10
Beta strandi227 – 231Combined sources5
Helixi237 – 249Combined sources13
Beta strandi257 – 264Combined sources8
Helixi265 – 281Combined sources17
Beta strandi285 – 288Combined sources4
Helixi290 – 295Combined sources6
Beta strandi299 – 301Combined sources3
Helixi304 – 306Combined sources3
Beta strandi313 – 323Combined sources11
Helixi324 – 334Combined sources11
Beta strandi337 – 343Combined sources7
Helixi347 – 356Combined sources10
Beta strandi359 – 366Combined sources8
Helixi368 – 370Combined sources3
Turni373 – 377Combined sources5
Beta strandi387 – 390Combined sources4
Helixi398 – 400Combined sources3
Beta strandi401 – 408Combined sources8

3D structure databases

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

CDDicd07079. ALDH_F18-19_ProA-GPR. 1 hit.
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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O20X-ray2.00A1-415[»]
ProteinModelPortaliQ9WYC9.
SMRiQ9WYC9.
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.
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

CDDicd07079. ALDH_F18-19_ProA-GPR. 1 hit.
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: November 2, 2016
This is version 131 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.