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B1Y8J5 (B1Y8J5_LEPCP) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Gamma-glutamyl phosphate reductase HAMAP MF_00412
Short name=GPR HAMAP MF_00412
EC=1.2.1.41 HAMAP MF_00412
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase HAMAP MF_00412
Glutamyl-gamma-semialdehyde dehydrogenase HAMAP MF_00412
Gene names
Name:proA HAMAP MF_00412
Ordered Locus Names:Lcho_4007
OrganismLeptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6)) [Complete proteome] [HAMAP] EMBL ACB36261.1
Taxonomic identifier395495 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Leptothrix

Protein attributes

Sequence length439 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. HAMAP MF_00412

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis HAMAP MF_00412
   Cellular componentCytoplasm HAMAP MF_00412
   LigandNADP HAMAP MF_00412
   Molecular functionOxidoreductase HAMAP MF_00412
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   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: HAMAP

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
B1Y8J5 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: F2599954000A615D

FASTA43946,243
        10         20         30         40         50         60 
MPRSAGLLCD NSGMNVLDIS AYMAHVGAAA RSASARMAAA TTAAKNRALL ALARRLREAG 

        70         80         90        100        110        120 
PALAEANARD LAAAEAAGLA GPMLDRLKLD AKAIATVAEG CEQLAAMPDP IGEILHLRQR 

       130        140        150        160        170        180 
PSGISVGQMR VPLGVFGMIY ESRPNVTIEA ASLAIKSGNA AILRGGSEAL HSNLALWKLV 

       190        200        210        220        230        240 
QAALTDAGLP AEAVQLVETT DRAAVGRLIA MPEYVDVIIP RGGKGLIERI SAEAKVPVIK 

       250        260        270        280        290        300 
HLDGNCHTYI DAQVDIEQAL VVTDNAKTQK YSPCNATESL LVHVEQAQAF LPRIGAIFAA 

       310        320        330        340        350        360 
KGVEMRCGPR AKAILSAVPG AKLVDATEAD WSEEYLAPII SIKLVDSLDD AIAHINRYSS 

       370        380        390        400        410        420 
HHTEAILTTS HPNAMRFLRE VDSASVMVNA STRFADGFEY GLGAEIGIST DKFHARGPVG 

       430 
LEGLTSLKYI VLGQGEVRG

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References

[1]"Complete sequence of Leptothrix cholodnii SP-6."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Emerson D., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001013 Genomic DNA. Translation: ACB36261.1.
RefSeqYP_001793026.1. NC_010524.1.

3D structure databases

ProteinModelPortalB1Y8J5.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1Y8J5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6160518.
GenomeReviewsGene locus Lcho_4007 in contig CP001013_GR.
KEGGlch:Lcho_4007.
PATRIC22398487. VBILepCho83238_4057.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG318080.
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.
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 nameB1Y8J5_LEPCP
AccessionPrimary (citable) accession number: B1Y8J5
Entry history
Integrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: December 14, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info