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C1D6E4 (PROA_LARHH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:LHK_03201
OrganismLaribacter hongkongensis (strain HLHK9) [Complete proteome] [HAMAP]
Taxonomic identifier557598 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeLaribacter

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
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 By similarity. 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 HAMAP MF_00412.

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 processproline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000193618

Sequences

Sequence LengthMass (Da)Tools
C1D6E4 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 8AACC75CBF64C70F

FASTA42044,547
        10         20         30         40         50         60 
MDLHSYMQDL GRAARAASRE LARADTRTKN AALLAMADAI ERDAAKLLAA NADDVKAAVA 

        70         80         90        100        110        120 
AGLAPAMVDR LTLTEKTVAG MAEGLRQIAS LPDPVGEMGE FAYRPSGIQL GKMRVPLGVI 

       130        140        150        160        170        180 
GIIYEARPNV TADAAGLCLK AGNACILRGG SEAFRSNQAI AACVHEGLAA ASLPTAAVQV 

       190        200        210        220        230        240 
LETTDRAAVG LLITMPEYVD VIVPRGGKGL IARISAEARV PVIKHLDGNC HTYVDVDADL 

       250        260        270        280        290        300 
EKALPVCDNA KTQRYGTCNT METLLVHEVV AEAFLPAICQ VYLDKGVELR GCATTRALIG 

       310        320        330        340        350        360 
ADKVQPATEE DWLTEYAAPI LAIKVIDSLD TAISHINHYG SHHTDVIITE NYSSARRFLR 

       370        380        390        400        410        420 
EVDSSSVMVN ASSRFADGFE YGLGAEIGIS TDKIHARGPV GLKGLTSEKW IVFGDGQVRG 

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References

[1]"The complete genome and proteome of Laribacter hongkongensis reveal potential mechanisms for adaptations to different temperatures and habitats."
Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L., Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J., Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.
PLoS Genet. 5:E1000416-E1000416(2009) [PubMed: 19283063] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HLHK9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001154 Genomic DNA. Translation: ACO76179.1.
RefSeqYP_002797188.1. NC_012559.1.

3D structure databases

ProteinModelPortalC1D6E4.
ModBaseSearch...

Protein-protein interaction databases

STRINGC1D6E4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7758808.
GenomeReviewsGene locus LHK_03201 in contig CP001154_GR.
KEGGlhk:LHK_03201.
PATRIC22303158. VBILarHon49832_2929.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYGICGAM.
ProtClustDBPRK00197.

Family and domain databases

HAMAPMF_00412. ProA.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR000965. G-glutamylP_reductase.
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. 2 hits.
KOK00147.
PANTHERPTHR11063:SF1. GSA_DH. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00407. ProA. 1 hit.
PROSITEPS01223. PROA. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_LARHH
AccessionPrimary (citable) accession number: C1D6E4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: January 25, 2012
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families