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A1TC11 (PROA_MYCVP) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 45. 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:Mvan_3934
OrganismMycobacterium vanbaalenii (strain DSM 7251 / PYR-1) [Complete proteome] [HAMAP]
Taxonomic identifier350058 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

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_1000049969

Sequences

Sequence LengthMass (Da)Tools
A1TC11 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 65FF58402747CB26

FASTA41543,291
        10         20         30         40         50         60 
MSVQAPSVPD LRQQVHDAAR RARGAARALA SLSTETKNRA LCTAADHVLM NTRTILDANT 

        70         80         90        100        110        120 
ADLDAARAAG TPEAMLDRLA LNPARVEGIA DGLRQVAGLP DPIGEVIRGR TLPNGLQLRQ 

       130        140        150        160        170        180 
QRVPLGVVGI VYEGRPNVTV DAFGLTLKSG NAVLLRGSSS AARSNAALVN ALRAALATEG 

       190        200        210        220        230        240 
LDTDAVQLLP SEDRASVTHL IQARGLVDVV IPRGGAGLID AVVRDAQVPT IETGVGNCHV 

       250        260        270        280        290        300 
FVHESADLDM AEEIVLNAKT RRPSVCNAAE SLLIDAAIAD VAVPRLTGAL TAAGVTVHAD 

       310        320        330        340        350        360 
PSEDELRAEF LSMDIALAIV DGVDGAISHI NEYGTGHTEA IVTTDLAAAQ RFSERVDAAA 

       370        380        390        400        410 
VMVNASTAFT DGEQFGFGAE IGISTQKLHA RGPMGLPELT STKWIVWGDG HTRPA 

« Hide

References

[1]"Complete sequence of Mycobacterium vanbaalenii PYR-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.J., Miller C., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 7251 / PYR-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000511 Genomic DNA. Translation: ABM14711.1.
RefSeqYP_954717.1. NC_008726.1.

3D structure databases

ProteinModelPortalA1TC11.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1TC11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000082930; EBMYCP00000080883; EBMYCG00000082925.
GeneID4646225.
GenomeReviewsGene locus Mvan_3934 in contig CP000511_GR.
KEGGmva:Mvan_3934.
PATRIC18186177. VBIMycVan31953_4002.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
GeneTreeEBGT00050000015663.
HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBA1TC11.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycMVAN350058:MVAN_3934-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. 1 hit.
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_MYCVP
AccessionPrimary (citable) accession number: A1TC11
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 45 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