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A3N3P3 (PROA_ACTP2) 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:APL_1951
OrganismActinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]
Taxonomic identifier416269 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length412 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 – 412412Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000049931

Sequences

Sequence LengthMass (Da)Tools
A3N3P3 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: AC22649C02FC1CE0

FASTA41244,907
        10         20         30         40         50         60 
MQMLTLAQQA KIASIELAQF GNVQKNHALL TIAEQLEQRS AEILAANAKD IEFAKNQGIS 

        70         80         90        100        110        120 
TAIIDRLLLN ESRLQGIAND VRNVAKLADP VGQVIDGGVL NSGLKIERQR VPLGVILTIY 

       130        140        150        160        170        180 
EARPNVTIDV ASLCLKTGNA VILRGGKETK FTNAVLVEVV QQALETAGLP KLAVQAVTDP 

       190        200        210        220        230        240 
DRALLLELLK LDRYIDMVIP RGGAGLHQFC KENSTIPVIV GGIGVCHMFV EKSADQEKAL 

       250        260        270        280        290        300 
ELIANAKTQR PSTCNTLETL LVEKAIAGEF LPKLANRMKA LDVTLHTDDL QKTEGIEPLD 

       310        320        330        340        350        360 
DARMRQEWLS LDLNVVVIDN LTKAVEHIRE YGSQHSEAIL TSDYQLARQF VAQVDAAAVY 

       370        380        390        400        410 
INASTRFTDG GEFGLGAEVA VSTQKLHARG PMGLEALTTY KWVCEGDYLV RK

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References

[1]"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)."
Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E.
J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000569 Genomic DNA. Translation: ABN75029.1.
RefSeqYP_001054634.1. NC_009053.1.

3D structure databases

ProteinModelPortalA3N3P3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3N3P3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4848580.
GenomeReviewsGene locus APL_1951 in contig CP000569_GR.
KEGGapl:APL_1951.
PATRIC20748996. VBIActPle94089_2031.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBA3N3P3.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycAPLE416269:APL_1951-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.
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_ACTP2
AccessionPrimary (citable) accession number: A3N3P3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 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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