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Q1B639 (PROA_MYCSS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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:Mmcs_3538
OrganismMycobacterium sp. (strain MCS) [Complete proteome] [HAMAP]
Taxonomic identifier164756 [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_1000049967

Sequences

Sequence LengthMass (Da)Tools
Q1B639 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: BB8F57C4F0A105AA

FASTA41543,482
        10         20         30         40         50         60 
MSVHAPAAPD LRTEVHDAAR RARVASRTLA TLSTETKNRA LRAAADRVLM DAHLIIAGNE 

        70         80         90        100        110        120 
RDLEKARAAG TPDAMLDRLA LNPQRIDGVA AGLRQVASLP DPVGEVLRGN TLVNGLQLRQ 

       130        140        150        160        170        180 
QRVPLGVVGI VYEGRPNVTV DAFGLTLKSG NAVLLRGSSS AAHSNAALVD SLRAALVAEG 

       190        200        210        220        230        240 
LDANAVQLLP SHDRASVTHL IQARGLVDVV IPRGGAGLID AVVRDAQVPT IETGVGNCHV 

       250        260        270        280        290        300 
YVHSAADLDM AETILLNAKT RRPSVCNAAE SVLIDAAIAE EAVPRLTKAL QDAGVTVHAD 

       310        320        330        340        350        360 
PTEEELRAEF LSMDIALAVV DGVDAAIAHV NEYGSGHTEA IVTADLAAAQ RFTERVDAAA 

       370        380        390        400        410 
VMVNASTAFT DGEQFGFGAE IGISTQKLHA RGPMGLPELT STKWIVWGDG HTRPA 

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium sp. MCS."
US DOE Joint Genome Institute
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., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000384 Genomic DNA. Translation: ABG09645.1.
RefSeqYP_640701.1. NC_008146.1.

3D structure databases

ProteinModelPortalQ1B639.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1B639.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000059242; EBMYCP00000057409; EBMYCG00000059237.
GeneID4112370.
GenomeReviewsGene locus Mmcs_3538 in contig CP000384_GR.
KEGGmmc:Mmcs_3538.
PATRIC18117373. VBIMycSp106721_3626.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
GeneTreeEBGT00050000015663.
HOGENOMHBG318080.
OMAQYPAACN.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycMSP164756:MMCS_3538-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.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_MYCSS
AccessionPrimary (citable) accession number: Q1B639
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: January 25, 2012
This is version 51 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