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C6EDK7 (C6EDK7_ECOBD) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 19. 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 EMBL ACT43466.1
Ordered Locus Names:B21_01598, ECBD_2005, ECD_01608
OrganismEscherichia coli (strain B / BL21-DE3) [Complete proteome] [HAMAP]
Taxonomic identifier469008 [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. SAAS SAAS019740 HAMAP MF_01629

Catalytic activity

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

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

Cofactor

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

Pathway

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

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

Subunit structure

Homodimer By similarity. SAAS SAAS019740 HAMAP MF_01629

Sequence similarities

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

Sequences

Sequence LengthMass (Da)Tools
C6EDK7 [UniParc].

Last modified September 1, 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].
Strain: B / BL21-DE3 [Korea].
[2]"Sequencing and gene expression analysis of Escherichia coli BL21."
Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [Austria].
[3]"Complete sequence of Escherichia coli BL21(DE3)."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [JGI].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001665 Genomic DNA. Translation: ACT29049.1.
CP001509 Genomic DNA. Translation: ACT43466.1.
AM946981 Genomic DNA. Translation: CAQ32115.1.

3D structure databases

ProteinModelPortalC6EDK7.
SMRC6EDK7. Positions 5-218.
ModBaseSearch...

Protein-protein interaction databases

STRINGC6EDK7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000156539; EBESCP00000146937; EBESCG00000159401.
EBESCT00000188384; EBESCP00000176391; EBESCG00000186953.
EBESCT00000193512; EBESCP00000182024; EBESCG00000193512.
GenomeReviewsGene locus B21_01598 in contig AM946981_GR.
Gene locus ECD_01608 in contig CP001509_GR.
Gene locus ECBD_2005 in contig CP001665_GR.
KEGGebd:ECBD_2005.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000008992.
OMAFTFFTNY.
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 nameC6EDK7_ECOBD
AccessionPrimary (citable) accession number: C6EDK7
Secondary accession number(s): C5W4L2
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: January 25, 2012
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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