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C9QRF4 (C9QRF4_ECOD1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
Short name=GPR HAMAP-Rule MF_00412
EC=1.2.1.41 HAMAP-Rule MF_00412
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase HAMAP-Rule MF_00412
Glutamyl-gamma-semialdehyde dehydrogenase HAMAP-Rule MF_00412
Gene names
Name:proA HAMAP-Rule MF_00412 EMBL BAJ42087.1
Ordered Locus Names:EcDH1_3364, ECDH1ME8569_0231 EMBL BAJ42087.1
OrganismEscherichia coli (strain ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1) [Complete proteome] [HAMAP] EMBL ACX40984.1
Taxonomic identifier536056 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length417 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 By similarity. HAMAP-Rule MF_00412 SAAS SAAS020593

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP-Rule MF_00412 SAAS SAAS020593

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP-Rule MF_00412 SAAS SAAS020593

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00412 SAAS SAAS020593.

Sequence similarities

Belongs to the gamma-glutamyl phosphate reductase family. HAMAP-Rule MF_00412

Sequences

Sequence LengthMass (Da)Tools
C9QRF4 [UniParc].

Last modified November 24, 2009. Version 1.
Checksum: D9A4E3418EFEB488

FASTA41744,630
        10         20         30         40         50         60 
MLEQMGIAAK QASYKLAQLS SREKNRVLEK IADELEAQSE IILNANAQDV ADARANGLSE 

        70         80         90        100        110        120 
AMLDRLALTP ARLKGIADDV RQVCNLADPV GQVIDGGVLD SGLRLERRRV PLGVIGVIYE 

       130        140        150        160        170        180 
ARPNVTVDVA SLCLKTGNAV ILRGGKETCR TNAATVAVIQ DALKSCGLPA GAVQAIDNPD 

       190        200        210        220        230        240 
RALVSEMLRM DKYIDMLIPR GGAGLHKLCR EQSTIPVITG GIGVCHIYVD ESVEIAEALK 

       250        260        270        280        290        300 
VIVNAKTQRP STCNTVETLL VNKNIADSFL PALSKQMAES GVTLHADAAA LAQLQAGPAK 

       310        320        330        340        350        360 
VVAVKAEEYD DEFLSLDLNV KIVSDLDDAI AHIREHGTQH SDAILTRDMR NAQRFVNEVD 

       370        380        390        400        410 
SSAVYVNAST RFTDGGQFGL GAEVAVSTQK LHARGPMGLE ALTTYKWIGI GDYTIRA

« Hide

References

[1]"Complete sequence of Escherichia coli DH1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Keasling J.D.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1.
[2]"Comparison of sequence reads obtained from three next-generation sequencing platforms."
Suzuki S., Ono N., Furusawa C., Ying B.W., Yomo T.
PLoS ONE 6:E19534-E19534(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1 and DH1 EMBL BAJ42087.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001637 Genomic DNA. Translation: ACX40984.1.
AP012030 Genomic DNA. Translation: BAJ42087.1.
RefSeqYP_006093273.1. NC_017625.1.
YP_006127632.1. NC_017638.1.

3D structure databases

SMRC9QRF4. Positions 16-416.
ModBaseSearch...

Proteomic databases

PRIDEC9QRF4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACX40984; ACX40984; EcDH1_3364.
BAJ42087; BAJ42087; ECDH1ME8569_0231.
GeneID12706991.
12873190.
KEGGedh:EcDH1_3364.
edj:ECDH1ME8569_0231.
PATRIC36699229. VBIEscCol36761_3558.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000246356.
KOK00147.
OMAEVGISTQ.

Enzyme and pathway databases

UniPathwayUPA00098; UER00360.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPMF_00412. ProA.
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]
PANTHERPTHR11063:SF1. PTHR11063:SF1. 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 nameC9QRF4_ECOD1
AccessionPrimary (citable) accession number: C9QRF4
Entry history
Integrated into UniProtKB/TrEMBL: November 24, 2009
Last sequence update: November 24, 2009
Last modified: May 1, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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