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A2SJZ5 (PDXH_METPP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Mpe_A2931
OrganismMethylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP]
Taxonomic identifier420662 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium

Protein attributes

Sequence length213 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-Rule MF_01629

Catalytic activity

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

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

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP-Rule MF_01629

Pathway

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

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01629

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Sequence caution

The sequence ABM95884.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   LigandFlavoprotein
FMN
   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: UniProtKB-HAMAP

pyridoxamine-phosphate oxidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000292303

Regions

Nucleotide binding77 – 782FMN By similarity
Nucleotide binding141 – 1422FMN By similarity
Region9 – 124Substrate binding By similarity
Region191 – 1933Substrate binding By similarity

Sites

Binding site621FMN By similarity
Binding site651FMN; via amide nitrogen By similarity
Binding site671Substrate By similarity
Binding site841FMN By similarity
Binding site1241Substrate By similarity
Binding site1281Substrate By similarity
Binding site1321Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A2SJZ5 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: 32016CE1032843D6

FASTA21324,309
        10         20         30         40         50         60 
MRPDIADLRK SYEQGELDEA HSAADPLQQF EQWLDQALKA KLPEPNAMTL ATVGADGRPS 

        70         80         90        100        110        120 
TRVVLIKGCD ARGIVWYTNY ESRKGRELAA HPFAALQFHW VDLERVVRIE GRVEKVSDTE 

       130        140        150        160        170        180 
SDAYYRSRPL DSRLGAWASP QSQVIASRAV LVANAAKVGA QFLLNPPRPP HWGGFRLRPD 

       190        200        210 
RWEFWQGRKS RLHDRLRYTQ QPTGGWLRER LAP 

« Hide

References

[1]"Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000555 Genomic DNA. Translation: ABM95884.1. Different initiation.
RefSeqYP_001022119.1. NC_008825.1.

3D structure databases

ProteinModelPortalA2SJZ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING420662.Mpe_A2931.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM95884; ABM95884; Mpe_A2931.
GeneID4784353.
KEGGmpt:Mpe_A2931.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycMPET420662:GHBE-2966-MONOMER.
UniPathwayUPA00190; UER00304.
UPA00190; UER00305.

Family and domain databases

Gene3D2.30.110.10. 1 hit.
HAMAPMF_01629. PdxH.
InterProIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERPTHR10851. PTHR10851. 1 hit.
PfamPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMSSF50475. SSF50475. 1 hit.
TIGRFAMsTIGR00558. pdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_METPP
AccessionPrimary (citable) accession number: A2SJZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways