Skip Header

Contribute Send feedback
Read comments (?) or add your own

A0AI64 (PROA_LISW6) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 42. 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:lwe1278
OrganismListeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334) [Complete proteome] [HAMAP]
Taxonomic identifier386043 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesListeriaceaeListeria

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_1000049961

Sequences

Sequence LengthMass (Da)Tools
A0AI64 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: A61437CB17D2C756

FASTA41545,776
        10         20         30         40         50         60 
MTELIKKGIA AREASSFLAQ ATTKQKNTAL INLSNDLIAN TATLLKENEK DIIRAKEKKT 

        70         80         90        100        110        120 
PDTMIDRLRL TEERIKEISE AVKQVVTLKD PIGEVTTMWK NEAELTIGKI RVPLGVIGII 

       130        140        150        160        170        180 
YESRPNVTVD ASILCFKTGN AVILRGGSDA IDSNKALMNV IQESLEKSGF PRTSVQLIED 

       190        200        210        220        230        240 
TSRETAREMM RLNRFLDVLI PRGGAKLIQT VLENATVPVI ETGTGNCHIY VDKAAEKQMA 

       250        260        270        280        290        300 
IDILVNAKCS RPSVCNSAET LLIHESVAED FLPAMEMALK EYNVELRADK RAREILKDAK 

       310        320        330        340        350        360 
AATESDWEEE FLDFILAIKV VDSVEEAINH INKYGTKHSE AIISNDYATG QAFHQKVDAA 

       370        380        390        400        410 
AVYINASTRF TDGFAMGFGA EIGISTQKLH ARGPMGLTEL TSTKYIIFGD GQIRN 

« Hide

References

[1]"Whole-genome sequence of Listeria welshimeri reveals common steps in genome reduction with Listeria innocua as compared to Listeria monocytogenes."
Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T. expand/collapse author list , Lampidis R., Kreft J., Goebel W., Chakraborty T.
J. Bacteriol. 188:7405-7415(2006) [PubMed: 16936040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35897 / DSM 20650 / SLCC5334.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM263198 Genomic DNA. Translation: CAK20696.1.
RefSeqYP_849475.1. NC_008555.1.

3D structure databases

ProteinModelPortalA0AI64.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0AI64.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4465449.
GenomeReviewsGene locus lwe1278 in contig AM263198_GR.
KEGGlwe:lwe1278.
NMPDRfig|386043.6.peg.1238.
PATRIC20329699. VBILisWel39304_1284.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBA0AI64.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycLWEL386043:LWE1278-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_LISW6
AccessionPrimary (citable) accession number: A0AI64
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 28, 2006
Last modified: December 14, 2011
This is version 42 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