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C6UIH9 (C6UIH9_ECOBR) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 17. 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:
Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629
EC=1.4.3.5 HAMAP MF_01629
Alternative name(s):
PNP/PMP oxidase HAMAP MF_01629
Pyridoxal 5'-phosphate synthase HAMAP MF_01629
Gene names
Name:pdxH HAMAP MF_01629
Ordered Locus Names:ECB_01608
OrganismEscherichia coli (strain B / REL606) [Complete proteome] [HAMAP] EMBL ACT39272.1
Taxonomic identifier413997 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) By similarity. HAMAP MF_01629 SAAS SAAS019740

Catalytic activity

Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. HAMAP MF_01629 SAAS SAAS019740

Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2. HAMAP MF_01629 SAAS SAAS019740

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_01629 SAAS SAAS019740

Pathway

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. HAMAP MF_01629 SAAS SAAS019740

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1. HAMAP MF_01629 SAAS SAAS019740

Subunit structure

Homodimer By similarity. HAMAP MF_01629 SAAS SAAS019740

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family. HAMAP MF_01629

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding82 – 832FMN By similarity HAMAP MF_01629
Nucleotide binding146 – 1472FMN By similarity HAMAP MF_01629
Region14 – 174Substrate binding By similarity HAMAP MF_01629
Region197 – 1993Substrate binding By similarity HAMAP MF_01629

Sites

Binding site671FMN By similarity HAMAP MF_01629
Binding site701FMN; via amide nitrogen By similarity HAMAP MF_01629
Binding site721Substrate By similarity HAMAP MF_01629
Binding site891FMN By similarity HAMAP MF_01629
Binding site1291Substrate By similarity HAMAP MF_01629
Binding site1331Substrate By similarity HAMAP MF_01629
Binding site1371Substrate By similarity HAMAP MF_01629

Sequences

Sequence LengthMass (Da)Tools
C6UIH9 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: 8B47CEEEA6CEF5F9

FASTA21825,545
        10         20         30         40         50         60 
MSDNDELQQI AHLRREYTKG GLRRRDLPAD PLTLFERWLS QACEAKLADP TAMVVATVDE 

        70         80         90        100        110        120 
HGQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS LLFPWHTLER QVMVIGKAER 

       130        140        150        160        170        180 
LSTLEVMKYF HSRPRDSQIG AWVSKQSSRI SARGILESKF LELKQKFQQG EVPLPSFWGG 

       190        200        210 
FRVSLEQIEF WQGGEHRLHD RFLYQRENDA WKIDRLAP

« Hide

References

[1]"Genome sequences of Escherichia coli B strains REL606 and BL21(DE3)."
Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.
J. Mol. Biol. 394:644-652(2009) [PubMed: 19786035] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000819 Genomic DNA. Translation: ACT39272.1.
RefSeqYP_003044808.1. NC_012967.1.

3D structure databases

ProteinModelPortalC6UIH9.
SMRC6UIH9. Positions 5-218.
ModBaseSearch...

Protein-protein interaction databases

STRINGC6UIH9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000161946; EBESCP00000151229; EBESCG00000162658.
GeneID8179054.
GenomeReviewsGene locus ECB_01608 in contig CP000819_GR.
KEGGebr:ECB_01608.
PATRIC18235302. VBIEscCol118196_1682.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000008992.
ProtClustDBPRK05679.

Family and domain databases

HAMAPMF_01629. PdxH.
[Tree]
InterProIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
IPR009002. Split_barrel_FMN-bd-related.
[Graphical view]
Gene3DG3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit.
KOK00275.
PANTHERPTHR10851. Pyridox_oxidase. 1 hit.
PfamPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMSSF50475. FMN_binding. 1 hit.
TIGRFAMsTIGR00558. PdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC6UIH9_ECOBR
AccessionPrimary (citable) accession number: C6UIH9
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: December 14, 2011
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info