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A5VSI3 (PROA_BRUO2) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 44. 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:BOV_1776
OrganismBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [Complete proteome] [HAMAP]
Taxonomic identifier444178 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length427 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 – 427427Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000193577

Sequences

Sequence LengthMass (Da)Tools
A5VSI3 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 9737335745912BFA

FASTA42744,729
        10         20         30         40         50         60 
MLVKADMTKD IAQVMAEVGR KAKAAAAPLS IATSEQKNKA LNAAADAILE ARADILEANR 

        70         80         90        100        110        120 
LDLANAEKNG MAASFVDRLT LNEARIDAIA EGIRTIATLP DPVGEVIAEW DRPNGLHIER 

       130        140        150        160        170        180 
VRTPLGVIGV IYESRPNVTA DAGALCLKAG NAVILRGGSD SAHSSAAIHK ALVKGLEAAN 

       190        200        210        220        230        240 
LPADAIQIVP VTDRAAVGEM LKGLGGAIDV IVPRGGKSLV ARVQSEARVP VFAHLEGICH 

       250        260        270        280        290        300 
LYIDKSADLD MARRIALDAK MRRTGICGAA ETLLVDRAVA STHLAPILGD LAAGGCEIRG 

       310        320        330        340        350        360 
SAEVLALYPA AKPATEEDWS TEYLDAIISV ALVDGISGAI DHINRYSSHH TEAIVAEDAQ 

       370        380        390        400        410        420 
TVARFFNEID SAILLHNAST QFADGGEFGM GAEIGIATGK MHARGPVGVE QLTSFKYRVR 


GSGQVRG

« Hide

References

[1]Paulsen I.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25840 / 63/290 / NCTC 10512.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000708 Genomic DNA. Translation: ABQ61250.1.
RefSeqYP_001259680.1. NC_009505.1.

3D structure databases

ProteinModelPortalA5VSI3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5VSI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5202138.
GenomeReviewsGene locus BOV_1776 in contig CP000708_GR.
KEGGbov:BOV_1776.
PATRIC17863643. VBIBruOvi136990_3204.
TIGRBOV_1776.

Phylogenomic databases

HOGENOMHBG318080.
OMAITHINRY.
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. 1 hit.
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_BRUO2
AccessionPrimary (citable) accession number: A5VSI3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 44 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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