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Reviewed, UniProtKB/Swiss-Prot Q9A2X6 (PROA_CAUCR)

Last modified June 16, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Gamma-glutamyl phosphate reductase
      Short name=GPR
    EC=1.2.1.41
Alternative name(s):
    Glutamate-5-semialdehyde dehydrogenase
    Glutamyl-gamma-semialdehyde dehydrogenase
      Short name=GSA dehydrogenase
Gene names
Name: proA
Ordered Locus Names: CC_3430
OrganismCaulobacter crescentus (Caulobacter vibrioides) [Complete proteome] [HAMAP]
Taxonomic identifier155892 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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. HAMAP MF_00412

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP MF_00412

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP MF_00412

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the gamma-glutamyl phosphate reductase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

proline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADP or NADPH binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 413413Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000189711

Sequences

Sequence LengthMass (Da)Tools
Q9A2X6-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 01D77D46F6EA38DC

FASTA41342,493
        10         20         30         40         50         60 
MAGMGRTARE GARALRLATP EQRTAAIQAM AVAIREDADA ILTANAKDLA RAEANGVSGP 

        70         80         90        100        110        120 
MLDRLALDAA RLEGVAAGVE AVAAVPDPVG VATSRWTRPN GLDIARVRTP IGVIAMIYES 

       130        140        150        160        170        180 
RPNVTADAAA LCVRSGNAVI LRGGSECIHS NLAIHAAIAR GLQKAGLPTA AVQAVKTPDR 

       190        200        210        220        230        240 
AAVGMILAGL DRTIDLIIPR GGKSLVARVQ AEARAPVLGH LEGLNHVFVH AAADLKKAVE 

       250        260        270        280        290        300 
VVVNAKLRRV SVCGSAETLL IDQAAADKLL PPIADALIKA GCELRGDAAA RAIEPTMKKA 

       310        320        330        340        350        360 
TVEDWTTEYL APILSVAVVD GVAGAARHIA SYGSGHTDAI ITEDAAAAEA FIAEVDSAIV 

       370        380        390        400        410 
LVNASTQFAD GGEFGFGAEI GIATDKLHAR GPVGAEQLTT FKYVVRGTGQ TRP 

« Hide

Cross-references

Sequence databases

AE005673 Genomic DNA. Translation: AAK25392.1.
PIRD87674.
RefSeqNP_422224.1.

3D structure databases

HSSPHSSP built from PDB template 1O20 based on UniProtKB Q9WYC9.
ModBaseSearch...

Genome annotation databases

GeneID940829.
GenomeReviewsGene locus CC_3430 in contig AE005673_GR.
KEGGccr:CC_3430.
NMPDRfig|190650.1.peg.3404.
TIGRCC_3430.

Phylogenomic databases

HOGENOMQ9A2X6.
OMAQ9A2X6. QYPAACN.

Enzyme and pathway databases

BRENDA1.2.1.41. 2191.

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR000965. Gglut_pp_reduct.
IPR012134. Glu-5-SA_DH.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11063:SF1. GSA_DH. 1 hit.
PIRSFPIRSF000151. GPR. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_CAUCR
AccessionPrimary (citable) accession number: Q9A2X6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents