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Q9KCR5 (PROA_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. 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:BH1504
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length416 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 – 416416Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000189691

Sequences

Sequence LengthMass (Da)Tools
Q9KCR5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 31502055CD267A4D

FASTA41645,423
        10         20         30         40         50         60 
MSELIEKAKQ AQQASKQLAI LTTEEKNRAL KQIADQLLVE RTYLIEENQK DIEAGQRAGI 

        70         80         90        100        110        120 
SQTLLDRLLL TDERVQAMAE GVEQVIALDD PIGDQIDEFT RPNGLNIRQV RVPLGVIGMI 

       130        140        150        160        170        180 
YEARPNVTVD ASVLCLKSGN AVLLRGSSSA LHSNKALVSV IHRGLEAANV IPKDAVQLLE 

       190        200        210        220        230        240 
DTSRETAKEM FKLNDYLDVL IPRGGANLIQ SVVKEASVPV LETGVGNCHV YIDESADPEM 

       250        260        270        280        290        300 
AVAIAVNAKT QRPSVCNAAE TILVHSAWAK EHVSKLIEEL RIKEVQIAGD EQIKAVAPFV 

       310        320        330        340        350        360 
KPADESDWGT EYLDLQVAMK IVNSVDEAIA HIDRYGSKHS EAIVSETDAN VRKFLTNVDA 

       370        380        390        400        410 
TTVYHNASTR FTDGFEFGFG AEIGISTQKL HARGPMGLRA LTSSKYVVHG TGQIKK 

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References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB05223.1.
PIRH83837.
RefSeqNP_242370.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KCR5.
SMRQ9KCR5. Positions 3-416.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000051867; EBBACP00000050506; EBBACG00000051858.
GeneID890633.
GenomeReviewsGene locus BH1504 in contig BA000004_GR.
KEGGbha:BH1504.
NMPDRfig|272558.1.peg.1504.
PATRIC18940104. VBIBacHal18977_1565.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000000020.
HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBQ9KCR5.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycBHAL272558:BH1504-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.
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_BACHD
AccessionPrimary (citable) accession number: Q9KCR5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 81 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