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P07004 (PROA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:b0243, JW0233
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 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
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processproline biosynthetic process

Inferred from genetic interaction Ref.1. Source: EcoCyc

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADP binding

Inferred from direct assay. Source: EcoCyc

glutamate-5-semialdehyde dehydrogenase activity

Inferred from direct assay. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000189723

Experimental info

Sequence conflict358 – 36710Missing Ref.1
Sequence conflict358 – 36710Missing Ref.2

Sequences

Sequence LengthMass (Da)Tools
P07004 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: D9A4E3418EFEB488

FASTA41744,630
        10         20         30         40         50         60 
MLEQMGIAAK QASYKLAQLS SREKNRVLEK IADELEAQSE IILNANAQDV ADARANGLSE 

        70         80         90        100        110        120 
AMLDRLALTP ARLKGIADDV RQVCNLADPV GQVIDGGVLD SGLRLERRRV PLGVIGVIYE 

       130        140        150        160        170        180 
ARPNVTVDVA SLCLKTGNAV ILRGGKETCR TNAATVAVIQ DALKSCGLPA GAVQAIDNPD 

       190        200        210        220        230        240 
RALVSEMLRM DKYIDMLIPR GGAGLHKLCR EQSTIPVITG GIGVCHIYVD ESVEIAEALK 

       250        260        270        280        290        300 
VIVNAKTQRP STCNTVETLL VNKNIADSFL PALSKQMAES GVTLHADAAA LAQLQAGPAK 

       310        320        330        340        350        360 
VVAVKAEEYD DEFLSLDLNV KIVSDLDDAI AHIREHGTQH SDAILTRDMR NAQRFVNEVD 

       370        380        390        400        410 
SSAVYVNAST RFTDGGQFGL GAEVAVSTQK LHARGPMGLE ALTTYKWIGI GDYTIRA 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the Escherichia coli proBA locus by DNA and protein sequencing."
Deutch A.H., Rushlow K.E., Smith C.J.
Nucleic Acids Res. 12:6337-6355(1984) [PubMed: 6089111] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 358-367.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Structure and biosynthesis of unbranched multicopy single-stranded DNA by reverse transcriptase in a clinical Escherichia coli isolate."
Lim D.
Mol. Microbiol. 6:3531-3542(1992) [PubMed: 1282191] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 368-417.
Strain: Clinical strain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00786 Genomic DNA. Translation: CAA25364.1.
U70214 Genomic DNA. Translation: AAB08663.1.
U00096 Genomic DNA. Translation: AAC73347.1.
AP009048 Genomic DNA. Translation: BAA77912.2.
Z12832 Genomic DNA. Translation: CAA78292.1.
PIRRDECER. D64749.
RefSeqNP_414778.1. NC_000913.2.

3D structure databases

ProteinModelPortalP07004.
SMRP07004. Positions 2-417.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10568N.
IntActP07004. 17 interactions.
MINTMINT-1261639.

2D gel databases

SWISS-2DPAGEP07004.
2DBase-EcoliP07004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000001314; EBESCP00000001314; EBESCG00000001089.
EBESCT00000016949; EBESCP00000016240; EBESCG00000016008.
GeneID946680.
GenomeReviewsGene locus JW0233 in contig AP009048_GR.
Gene locus b0243 in contig U00096_GR.
KEGGecj:JW0233.
eco:b0243.
PATRIC32115601. VBIEscCol129921_0245.

Organism-specific databases

EchoBASEEB0760.
EcoGeneEG10767. proA.

Phylogenomic databases

eggNOGCOG0014.
GeneTreeEBGT00050000009178.
HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBP07004.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycEcoCyc:GLUTSEMIALDEHYDROG-MONOMER.
MetaCyc:GLUTSEMIALDEHYDROG-MONOMER.

Gene expression databases

GenevestigatorP07004.

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. 1 hit.
[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_ECOLI
AccessionPrimary (citable) accession number: P07004
Secondary accession number(s): P77428
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families