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C9QUU5 (C9QUU5_ECOD1) 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 BAJ43438.1
Ordered Locus Names:EcDH1_2002
ORF Names:ECDH1ME8569_1582 EMBL BAJ43438.1
OrganismEscherichia coli (strain ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1) [Complete proteome] [HAMAP] EMBL ACX39659.1
Taxonomic identifier536056 [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
C9QUU5 [UniParc].

Last modified November 24, 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

« Hide 'large scale' references
[1]"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: 21611185] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DH1 EMBL BAJ43438.1.
[2]"Complete sequence of Escherichia coli DH1."
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001637 Genomic DNA. Translation: ACX39659.1.
AP012030 Genomic DNA. Translation: BAJ43438.1.

3D structure databases

ProteinModelPortalC9QUU5.
SMRC9QUU5. Positions 5-218.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000198720; EBESCP00000187718; EBESCG00000199129.
GenomeReviewsGene locus EcDH1_2002 in contig CP001637_GR.
PATRIC36696298. VBIEscCol36761_2116.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000008992.
OMAFTFFTNY.

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.
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 nameC9QUU5_ECOD1
AccessionPrimary (citable) accession number: C9QUU5
Entry history
Integrated into UniProtKB/TrEMBL: November 24, 2009
Last sequence update: November 24, 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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