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A1KTV4 (PROA_NEIMF) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 46. 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:NMC1032
OrganismNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / FAM18) [Complete proteome] [HAMAP]
Taxonomic identifier272831 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length420 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 – 420420Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000049970

Sequences

Sequence LengthMass (Da)Tools
A1KTV4 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 0FE46B0DEA976FAA

FASTA42044,928
        10         20         30         40         50         60 
MSNTQKQLAL AKAAKKSVNT ADTEEKNRAL LAMADSLEAA AADILAANRQ DLEAAAGKIP 

        70         80         90        100        110        120 
ESMTDRLLLD GKRICAMADG IRAVAALPDP VGEILETSTL PNGLEIVKKR VAMGVIGIIY 

       130        140        150        160        170        180 
ESRPNVTSDA AALALKSGSA VVLRSGKDAF QSARAIVAAL KTGLAQTRID PDALQLIEDT 

       190        200        210        220        230        240 
GREGSYEMMR AKDYLDLLIP RGGAGLIRAV VENAVVPVIE TGTGIVHIYV DKDADLEKAI 

       250        260        270        280        290        300 
RIVRNAKTSR PSVCNSMEVL LVHEDIAADF LPKLERLLVR DRIEAGLPPV RFRLDPQAAR 

       310        320        330        340        350        360 
HIGGEAAGAD DFDTEFLDYI LAVKTVASVE EAVGHIEAHG THHSDGIVTE NRHAADYFTT 

       370        380        390        400        410        420 
HIDSAAVYVN ASTRFTDGGE FGLGCEMGIS TQKLHARGPM GLKELTSYKY IVQGTGQVRE 

« Hide

References

[1]"Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18."
Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., Quail M.A., Achtman M. expand/collapse author list , Barrell B.G., Saunders N.J., Parkhill J.
PLoS Genet. 3:230-240(2007) [PubMed: 17305430] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700532 / FAM18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM421808 Genomic DNA. Translation: CAM10294.1.
RefSeqYP_975083.1. NC_008767.1.

3D structure databases

ProteinModelPortalA1KTV4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1KTV4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBNEIT00000008690; EBNEIP00000008459; EBNEIG00000008690.
GeneID4675630.
GenomeReviewsGene locus NMC1032 in contig AM421808_GR.
KEGGnmc:NMC1032.
NMPDRfig|487.2.peg.2023.
PATRIC20352007. VBINeiMen17609_1256.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
GeneTreeEBGT00050000020602.
HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBA1KTV4.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycNMEN272831:NMC1032-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. 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_NEIMF
AccessionPrimary (citable) accession number: A1KTV4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 46 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