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A5U5C2 (PROA_MYCTA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 41. 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:MRA_2453
OrganismMycobacterium tuberculosis (strain ATCC 25177 / H37Ra) [Complete proteome] [HAMAP]
Taxonomic identifier419947 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length415 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 – 415415Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000049968

Sequences

Sequence LengthMass (Da)Tools
A5U5C2 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 071C9872F8C9A8AC

FASTA41543,745
        10         20         30         40         50         60 
MTVPAPSQLD LRQEVHDAAR RARVAARRLA SLPTTVKDRA LHAAADELLA HRDQILAANA 

        70         80         90        100        110        120 
EDLNAAREAD TPAAMLDRLS LNPQRVDGIA AGLRQVAGLR DPVGEVLRGY TLPNGLQLRQ 

       130        140        150        160        170        180 
QRVPLGVVGM IYEGRPNVTV DAFGLTLKSG NAALLRGSSS AAKSNEALVA VLRTALVGLE 

       190        200        210        220        230        240 
LPADAVQLLS AADRATVTHL IQARGLVDVV IPRGGAGLIE AVVRDAQVPT IETGVGNCHV 

       250        260        270        280        290        300 
YVHQAADLDV AERILLNSKT RRPSVCNAAE TLLVDAAIAE TALPRLLAAL QHAGVTVHLD 

       310        320        330        340        350        360 
PDEADLRREY LSLDIAVAVV DGVDAAIAHI NEYGTGHTEA IVTTNLDAAQ RFTEQIDAAA 

       370        380        390        400        410 
VMVNASTAFT DGEQFGFGAE IGISTQKLHA RGPMGLPELT STKWIAWGAG HTRPA 

« Hide

References

[1]"Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra, a non-pathogenic variant closely related to the well-characterized pathogenic strain H37Rv."
Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y., Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25177 / H37Ra.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000611 Genomic DNA. Translation: ABQ74222.1.
RefSeqYP_001283784.1. NC_009525.1.

3D structure databases

ProteinModelPortalA5U5C2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5U5C2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000067775; EBMYCP00000065885; EBMYCG00000067770.
GeneID5214579.
GenomeReviewsGene locus MRA_2453 in contig CP000611_GR.
KEGGmra:MRA_2453.
PATRIC18145118. VBIMycTub106795_2757.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
GeneTreeEBGT00050000015663.
HOGENOMHBG318080.
OMAQYPAACN.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycMTUB419947:MRA_2453-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. 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_MYCTA
AccessionPrimary (citable) accession number: A5U5C2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 41 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