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Q5QTW7 (PDXH_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:IL1209
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length212 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.

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 – 212212Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167713

Regions

Nucleotide binding76 – 772FMN By similarity
Nucleotide binding140 – 1412FMN By similarity
Region7 – 104Substrate binding By similarity
Region191 – 1933Substrate binding By similarity

Sites

Binding site611FMN By similarity
Binding site641FMN; via amide nitrogen By similarity
Binding site661Substrate By similarity
Binding site831FMN By similarity
Binding site1231Substrate By similarity
Binding site1271Substrate By similarity
Binding site1311Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5QTW7 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: CC58974FD7716DEB

FASTA21224,824
        10         20         30         40         50         60 
MDLQAMRREY GLGSLHREQL EADPVKQFEK WMQQAIDSNL LSDPTAMTLA TVDAEHMPSQ 

        70         80         90        100        110        120 
RIVLLKGYDH TGFRFYTNKN SHKGQDISEN PQVALHFAWL PLERQISIIG SAVPLDDDDN 

       130        140        150        160        170        180 
DRYFHSRPKE SQVAALASQQ SRPVESRDVL ESHYQSLLKD YENTEVPRPQ SWGGYCVHPK 

       190        200        210 
QFEFWQGGQH RLHDRYQYSK DRENWRITRL QP 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV82049.1.
RefSeqYP_155598.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QTW7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL1209.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV82049; AAV82049; IL1209.
GeneID3174172.
KEGGilo:IL1209.
PATRIC22140489. VBIIdiLoi21852_1210.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAELDHRGF.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycILOI283942:GI0U-1217-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_IDILO
AccessionPrimary (citable) accession number: Q5QTW7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 70 of the entry and version 1 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