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B7I5F5 (PROA_ACIB5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:AB57_0592
OrganismAcinetobacter baumannii (strain AB0057) [Complete proteome] [HAMAP]
Taxonomic identifier480119 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

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 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 – 421421Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000123766

Sequences

Sequence LengthMass (Da)Tools
B7I5F5 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: BB9D19EFB27D1943

FASTA42145,687
        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 LRGCPETRRI 

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

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


Q 

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References

[1]"Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii."
Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., Bonomo R.A., Gill S.R.
J. Bacteriol. 190:8053-8064(2008) [PubMed: 18931120] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AB0057.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001182 Genomic DNA. Translation: ACJ40013.1.
RefSeqYP_002317996.1. NC_011586.1.

3D structure databases

ProteinModelPortalB7I5F5.
SMRB7I5F5. Positions 14-421.
ModBaseSearch...

Protein-protein interaction databases

STRINGB7I5F5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7043642.
GenomeReviewsGene locus AB57_0592 in contig CP001182_GR.
KEGGabn:AB57_0592.
PATRIC20694991. VBIAciBau111166_0580.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG318080.
OMAQYPAACN.
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 namePROA_ACIB5
AccessionPrimary (citable) accession number: B7I5F5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 24 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