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P54903 (PROA_THET2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. 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:TT_C1564
OrganismThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]
Taxonomic identifier262724 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length413 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

Sequence similarities

Belongs to the gamma-glutamyl phosphate reductase family.

Sequence caution

The sequence BAA06238.1 differs from that shown. Reason: Frameshift at position 389.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 413413Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000189803

Sequences

Sequence LengthMass (Da)Tools
P54903 [UniParc].

Last modified May 24, 2004. Version 3.
Checksum: EC63FDFF0FC2B71E

FASTA41345,851
        10         20         30         40         50         60 
MTATSLWELA ERARKRLSEI AKGNRDRALL AMADLLEARW EEVLRANRED LEEAERTGLP 

        70         80         90        100        110        120 
KAKLDRLALK EKDLKTLTEG LRQIARLPDP LGRIEGLAKR PNGLRVGRMR VPLGLIGFIY 

       130        140        150        160        170        180 
EARPGATVEA VSVALKAGNA MLLRGGKEAF RSNRALVALW HEALEEAGLP EEAVTLVPTT 

       190        200        210        220        230        240 
DREAVLEMCR LELLDLLIPR GGEELIRLVQ QEARVPVLAH AKGVNHLYVD EKADLSMALR 

       250        260        270        280        290        300 
LALNGKTQRP AVCNALEAVL VHEKVAEAFL PRLEKAMREK GVELRACPRA LPLLKEAVPA 

       310        320        330        340        350        360 
REDEWDREYL DLVLRVKVVS GLEEALAHIA RYGSRHTEAI CTEDPKAAWR FLEEVDASLV 

       370        380        390        400        410 
LWNASTRFND GFELGLGAEI GISTSKLHAY GPMGPLELTT LKWVALGEGQ ERT 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequence analysis of the proBA operon from an extremely thermophilic eubacterium Thermus thermophilus."
Kosuge T., Tabata K., Hoshino T.
FEMS Microbiol. Lett. 123:55-61(1994) [PubMed: 7988899] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of the extreme thermophile Thermus thermophilus."
Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.
Nat. Biotechnol. 22:547-553(2004) [PubMed: 15064768] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB27 / ATCC BAA-163 / DSM 7039.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D29973 Genomic DNA. Translation: BAA06238.1. Frameshift.
AE017221 Genomic DNA. Translation: AAS81906.1.
RefSeqYP_005533.1. NC_005835.1.

3D structure databases

ProteinModelPortalP54903.
ModBaseSearch...

Protein-protein interaction databases

STRINGP54903.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2775994.
GenomeReviewsGene locus TT_C1564 in contig AE017221_GR.
PATRIC23953565. VBITheThe54392_1560.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
PhylomeDBP54903.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycTTHE262724:TT_C1564-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.
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_THET2
AccessionPrimary (citable) accession number: P54903
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 24, 2004
Last modified: January 25, 2012
This is version 87 of the entry and version 3 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