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A1BAM3 (PROA_PARDP) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 42. 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:Pden_4503
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Protein attributes

Sequence length423 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 – 423423Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000340901

Sequences

Sequence LengthMass (Da)Tools
A1BAM3 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: DB36C9DB8A4D063B

FASTA42344,707
        10         20         30         40         50         60 
MKDLTSSDAD ALIADLGQKA RAAAAVLAEA SAERKHAALI GAADAILEAE DAILDANAED 

        70         80         90        100        110        120 
MHYAEEKGLS PAMLDRLKLD PARIRAMAEG LRSVAAQADP VGKVLAEWDR PNGLNIRRVA 

       130        140        150        160        170        180 
TPLGVIGVVY ESRPNVTADA AALALKAGNA VILRGGSESL NSSAAIHRAL VTGLKQAGLP 

       190        200        210        220        230        240 
ETAIQMVPTR DREAVAAMLR AQDYIDVIVP RGGKGLVGLV QKEARVPVFA HLEGICHVYA 

       250        260        270        280        290        300 
DRDADLDKAR RVVLNAKTRR TGICGAAECL LIDWQFYTKH GPVLVQDLLD AGVEVRAEGE 

       310        320        330        340        350        360 
LAKVPGTVPA EPSDFGQEFL DKIIAVKLVD GVEEAIAHIR RHGSGHTESI LTENDATAER 

       370        380        390        400        410        420 
FFSGLDSAIL MRNASTQFAD GGEFGMGAEI GIATGKMHAR GPVGAEQLTS FKYLVTGDGT 


IRP

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References

[1]"Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000490 Genomic DNA. Translation: ABL72567.1.
RefSeqYP_918263.1. NC_008687.1.

3D structure databases

ProteinModelPortalA1BAM3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1BAM3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4583053.
GenomeReviewsGene locus Pden_4503 in contig CP000490_GR.
KEGGpde:Pden_4503.
PATRIC22860228. VBIParDen97112_4466.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
PhylomeDBA1BAM3.
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. 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_PARDP
AccessionPrimary (citable) accession number: A1BAM3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 42 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

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