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Q73XR2 (PROA_MYCPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. 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:MAP_2247c
OrganismMycobacterium paratuberculosis [Complete proteome] [HAMAP]
Taxonomic identifier1770 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length435 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 – 435435Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000189752

Sequences

Sequence LengthMass (Da)Tools
Q73XR2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6B809138D15EC5F3

FASTA43545,525
        10         20         30         40         50         60 
MGLQAPFRSG GGTSRPQGRA APRAVDLRRE VHDAARRARV ASRVLALLPA VAKDQALRSA 

        70         80         90        100        110        120 
ADAIAGHAEL ILSANAEDLE TARAAGTPSA MLDRLALDTK RVEGIAAGLR QVAGLPDPVG 

       130        140        150        160        170        180 
EVLRGYTLPN GLQLRQQRVP LGVVGMIYEG RPNVTVDAFG LALKSGNAVL LRGSSSATRS 

       190        200        210        220        230        240 
NQALVQVLRA SLVSEDLPAD AVQLLSADDR ATVTHLIQAR GLVDVVIPRG GANLINAVVR 

       250        260        270        280        290        300 
DAQVPTIETG VGNCHVYVHE GADLEVAERV LLNSKTRRPS VCNAAETLLV DAAIAEEALP 

       310        320        330        340        350        360 
RLVTALQDAG VTVHGGFARD ATEDDLRREY LSMDIAVAVV DGVDAAIAHI NEYGTGHTEA 

       370        380        390        400        410        420 
IVTTNMAAAQ RFTDGVDAAA VMVNASTAFT DGEQFGFGAE IGISTQKLHA RGPMGLPELT 

       430 
STKWIAWGDG QTRPA 

« Hide

References

[1]"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed: 16116077] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-968 / K-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016958 Genomic DNA. Translation: AAS04564.1.
RefSeqNP_961181.1. NC_002944.2.

3D structure databases

ProteinModelPortalQ73XR2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000038060; EBMYCP00000036449; EBMYCG00000038055.
GeneID2718562.
GenomeReviewsGene locus MAP_2247c in contig AE016958_GR.
KEGGmpa:MAP2247c.
NMPDRfig|262316.1.peg.2247.
PATRIC17997132. VBIMycAvi108102_2390.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000015663.
HOGENOMHBG318080.
OMAQYPAACN.
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. 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_MYCPA
AccessionPrimary (citable) accession number: Q73XR2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 61 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