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Q2IHV2 (PDXH_ANADE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyridoxine/pyridoxamine 5'-phosphate oxidase
EC=1.4.3.5
Alternative name(s):
PNP/PMP oxidase
Short name=PNPOx
Pyridoxal 5'-phosphate synthase
Gene names
Name:pdxH
Ordered Locus Names:Adeh_1455
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

Protein attributes

Sequence length198 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

Catalytic activity

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

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

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_01629

Pathway

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

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

Subunit structure

Homodimer By similarity. HAMAP MF_01629

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFMN binding

Inferred from electronic annotation. Source: InterPro

pyridoxamine-phosphate oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 198198Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629
PRO_0000255851

Regions

Nucleotide binding62 – 632FMN By similarity
Nucleotide binding126 – 1272FMN By similarity
Region177 – 1793Substrate binding By similarity

Sites

Binding site471FMN By similarity
Binding site501FMN; via amide nitrogen By similarity
Binding site521Substrate By similarity
Binding site691FMN By similarity
Binding site1091Substrate By similarity
Binding site1131Substrate By similarity
Binding site1171Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2IHV2 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 3A32F2623434D844

FASTA19821,612
        10         20         30         40         50         60 
MPLPPSAAPD PIARFRDALA RAAAASPHDA TAAALATADA RGAPSVRMVL VKSADARGFA 

        70         80         90        100        110        120 
FFTNRESRKA RDLAANPRAA LCFHWPALEE QVRVEGAVTP LPDAEADAYF RSRPRESRVG 

       130        140        150        160        170        180 
AWASRQSAPL GDRAELEAAV REVEARFPGD EIPRPPFWGG YLVAPERIEF WRSGPGRLHH 

       190 
RTVYVRRGDG WEVGALQP

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000251 Genomic DNA. Translation: ABC81228.1.
RefSeqYP_464665.1. NC_007760.1.

3D structure databases

ProteinModelPortalQ2IHV2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2IHV2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3887698.
GenomeReviewsGene locus Adeh_1455 in contig CP000251_GR.
KEGGade:Adeh_1455.
PATRIC20919031. VBIAnaDeh31384_1506.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHBG327559.
OMAHWSGFRI.
PhylomeDBQ2IHV2.
ProtClustDBCLSK945648.

Enzyme and pathway databases

BioCycADEH290397:ADEH_1455-MONOMER.

Family and domain databases

HAMAPMF_01629. PdxH.
[Tree]
InterProIPR000659. Pyridox_Oxase.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_ANADE
AccessionPrimary (citable) accession number: Q2IHV2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 44 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

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