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A1TVU4 (PROA_ACIAC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Aave_4545
OrganismAcidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length426 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. 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 – 426426Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000049929

Sequences

Sequence LengthMass (Da)Tools
A1TVU4 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: CD037332B397AAA4

FASTA42645,427
        10         20         30         40         50         60 
MNAQHIAETL HALGSQAKAA SALMARAPSA VKNRALLALA RRLRDNTTAL QADNARDLER 

        70         80         90        100        110        120 
ARAAGLAEPM VDRLKLTPKV LETCALGCEQ LATMGDVIGE ISGMRQQPSG IRVGQMRVPI 

       130        140        150        160        170        180 
GVFGMIYESR PNVTIEAASL SIKSGNACIL RGGSEAIDSN RALARLVQEA LEEAGLPGDA 

       190        200        210        220        230        240 
VQLVQTTDRE AVGHLIAMPQ YVDVIIPRGG KGLIERISRD AKVPVIKHLD GNCHTYVDDP 

       250        260        270        280        290        300 
CDVAMAVKVA DNAKTQKYSP CNASEGLLVA RGVAAEFLPR IGAVYAAKGV EMRGCPETLA 

       310        320        330        340        350        360 
LLAGVPGATL VHATEQDWSE EYLAPIISIK VVEGLDEAIA HINRYGSHHT DAILTRDHMH 

       370        380        390        400        410        420 
AQRFLREVDS ASVMVNASTR FADGFEYGLG AEIGISTDKF HARGPVGIEG LTSLKWVVLG 


EGDIRA 

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References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AAC00-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000512 Genomic DNA. Translation: ABM35082.1.
RefSeqYP_972856.1. NC_008752.1.

3D structure databases

ProteinModelPortalA1TVU4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1TVU4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4667910.
GenomeReviewsGene locus Aave_4545 in contig CP000512_GR.
KEGGaav:Aave_4545.
NMPDRfig|397945.5.peg.3914.
PATRIC20684349. VBIAciCit38535_4624.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
PhylomeDBA1TVU4.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycAAVE397945:AAVE_4545-MONOMER.

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.
IPR020593. G-glutamylP_reductase_CS.
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. 2 hits.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00407. ProA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_ACIAC
AccessionPrimary (citable) accession number: A1TVU4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 47 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