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Reviewed, UniProtKB/Swiss-Prot B0VKT1 (PROA_ACIBS)

Last modified February 9, 2010. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: ABSDF3014
OrganismAcinetobacter baumannii (strain SDF) [Complete proteome] [HAMAP]
Taxonomic identifier509170 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length421 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 processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

proline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADP or NADPH binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000123768

Sequences

Sequence LengthMass (Da)Tools
B0VKT1-1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: CC88F9E755654E46

FASTA42145,696
        10         20         30         40         50         60 
MQDSIEQYMQ KVGQQARDAS RVLTSASTSL KNHALSAIYT ALENNQAAIL AANQIDMEKG 

        70         80         90        100        110        120 
RSNQLDSALL DRLELTPARF KGMLQGLKDV IALVDPIGEI TDLAYRPTGI QIGKMRVPLG 

       130        140        150        160        170        180 
VVGMIYESRP NVTLEAASLA IKSGNAIILR GGSEALESNK AIAEAVKHGL KVAGLPEHSV 

       190        200        210        220        230        240 
QVIETSDRAA VGHLITMAEY VDVIVPRGGK SLIERVTNEA RIPVIKHLDG NCHVFVEAQA 

       250        260        270        280        290        300 
DLQKALPITL NAKTHRYGVC NAMETLLVDE KIAEVFLPHI AELYAEKQVE LRGCPETHRI 

       310        320        330        340        350        360 
LGTTVKPATE EDWYTEYLGP ILAVKVVSGI DEAIDHINKY GSHHTDAIVT ENYTLARQFL 

       370        380        390        400        410        420 
ARVDSSSVVV NASTRFADGF EYGLGAEIGI STDKIHARGP VGLEGLTSQK WIVLGDGQIR 


Q 

« Hide

References

[1]"Comparative analysis of Acinetobacters: three genomes for three lifestyles."
Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S.
PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU468230 Genomic DNA. Translation: CAP02300.1.
RefSeqYP_001708152.1.

3D structure databases

SMRB0VKT1. Positions 14-421.
ModBaseSearch...

Genome annotation databases

GeneID5986001.
GenomeReviewsGene locus ABSDF3014 in contig CU468230_GR.
KEGGabm:ABSDF3014.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG318080.
OMAQYPAACN.

Family and domain databases

HAMAPMF_00412. ProA.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
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. 1 hit.
PANTHERPTHR11063:SF1. GSA_DH. 1 hit.
PfamPF00171. Aldedh. 2 hits.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_ACIBS
AccessionPrimary (citable) accession number: B0VKT1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 8, 2008
Last modified: February 9, 2010
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents