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Reviewed, UniProtKB/Swiss-Prot Q3AF39 (PROA_CARHZ)

Last modified November 25, 2008. Version 24. 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: CHY_0383
OrganismCarboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [Complete proteome] [HAMAP]
Taxonomic identifier246194 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteriaceaeCarboxydothermus

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH.

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.

Subcellular location

CytoplasmBy similarity.

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: HAMAP

   Molecular functionNADP 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 – 415415Gamma-glutamyl phosphate reductase
PRO_0000229996

Sequences

Sequence LengthMass (Da)Tools
Q3AF39-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 2F0BED5AA870B69D

FASTA41545,489
        10         20         30         40         50         60 
MDEVLNLAKK AKEASKKLAQ LSTEQKNRAL LKIAQYLEEN MEKILTENQK DLAEAKKGGL 

        70         80         90        100        110        120 
SPAFIERLTL NEKRILDMAE GVRQVAKLPD PVGEVLGMTR RPNGLVIGQV RVPLGVVGII 

       130        140        150        160        170        180 
YESRPNVTVD AAALCLKAGN AVILRGGKEA FNSNLALVTL MEEALRSEEI PEGAVGMIKT 

       190        200        210        220        230        240 
TSRDAANYLM RLNGYLDVLI PRGGAGLIKT VVENSTVPVI ETGVGNCHVY VEEDADLEMA 

       250        260        270        280        290        300 
ERIIINAKCQ RPAVCNAMET LLVHEKIAPV FLPQIGKALK ENGVEIRGCE VTRRYIPDAL 

       310        320        330        340        350        360 
PATEEDYYTE FLDLILAVRV VRDLDEAIAH ITKYGSGHSE AIVTRDYFKA RRFTEEVDAA 

       370        380        390        400        410 
AVYVNASTRF TDGFEFGFGA EIGISTQKLH ARGPMGLKEL TTTKYVIYGT GQIRG 

« Hide

References

[1]"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901."
Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.
PLoS Genet. 1:563-574(2005) [PubMed: 16311624] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000141 Genomic DNA. Translation: ABB13750.1.
RefSeqYP_359245.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3726908.
GenomeReviewsGene locus CHY_0383 in contig CP000141_GR.
KEGGchy:CHY_0383.
NMPDRfig|246194.3.peg.599.
TIGRCHY_0383.

Phylogenomic databases

HOGENOMQ3AF39.

Enzyme and pathway databases

BioCycCHYD246194:CHY_0383-MON.

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016163. Ald_DHase_C.
IPR016162. Ald_DHase_N.
IPR015590. Aldehyde_DHase.
IPR000965. Gglut_pp_reduct.
IPR012134. Glu-5-SA_DHase.
[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. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_CARHZ
AccessionPrimary (citable) accession number: Q3AF39
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 22, 2005
Last modified: November 25, 2008
This is version 24 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