Skip Header

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

Q6NFW0 (PROA_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. 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:DIP1776
OrganismCorynebacterium diphtheriae [Complete proteome] [HAMAP]
Taxonomic identifier1717 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length430 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 – 430430Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000189717

Sequences

Sequence LengthMass (Da)Tools
Q6NFW0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E59CA38085F50DE8

FASTA43045,150
        10         20         30         40         50         60 
MLMNNADVRS QERKQVMVCA RAAHRVAPIV AQLTSADKNA VLLDAAAALE AAGAEIIAAN 

        70         80         90        100        110        120 
QRDIDQGRAR GLSEALIDRL SLDSARIAGI AGGLRQVAAL SDPVGEVVGG SVMPNGMQMR 

       130        140        150        160        170        180 
KVRVPLGVMG MVYEARPNVT IDAFGLALKS GNVALLRGSK SAQHSNAALV AVVHRVLESH 

       190        200        210        220        230        240 
GLPHEVVQLL PCETHESVQD LITARGLVDV VIPRGGAGLI EAVVTNATVP TIETGTGNCH 

       250        260        270        280        290        300 
FYIDRDVSDL DQAIAMLLNG KTRRCSVCNA TETVLIDSAL DSAYQLAIIT ALQEAGVTVH 

       310        320        330        340        350        360 
GDVAQLEAVG ASGIVPADEH DWAEEYLSLD IACALVDGVD AAMEHIRTYS TKHTEAIATG 

       370        380        390        400        410        420 
NIVTAQRFAD RVDAAAVMIN ASTAFTDGEQ FGMGAEIGIS TQKLHARGPM ALPELTTTKW 

       430 
IVQGTGQTRP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248359 Genomic DNA. Translation: CAE50306.1.
RefSeqNP_940114.1. NC_002935.2.

3D structure databases

ProteinModelPortalQ6NFW0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2649401.
GenomeReviewsGene locus DIP1776 in contig BX248353_GR.
KEGGcdi:DIP1776.
NMPDRfig|257309.1.peg.1705.
PATRIC21484778. VBICorDip47633_1762.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBQ6NFW0.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycCDIP257309:DIP1776-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_CORDI
AccessionPrimary (citable) accession number: Q6NFW0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 60 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