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B8EAI0 (PDXH_SHEB2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 35. 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:Sbal223_2515
OrganismShewanella baltica (strain OS223) [Complete proteome] [HAMAP]
Taxonomic identifier407976 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

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_1000186341

Regions

Nucleotide binding76 – 772FMN By similarity
Nucleotide binding140 – 1412FMN By similarity
Region8 – 114Substrate 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
B8EAI0 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 806C015C9E55528D

FASTA21224,330
        10         20         30         40         50         60 
MTDLSDIRRE YAKGGLRRAD LPQNPMDLFE LWMTQARDAE LSDPTAMCVA TVDEHGQPFQ 

        70         80         90        100        110        120 
RIVLLKRFDD TGFVFFTNLG SRKAQQIAAN NKVSLHFPWH PLERQVSVLG EAQALSTAEV 

       130        140        150        160        170        180 
LKYFMTRPKD SQIAAWVSQQ SSKLSARQVL EGKFFEMKAK FAKGDVPLPS FWGGYLVRPS 

       190        200        210 
SIEFWQGGEH RLHDRFIYAR HDAEWEIDRL AP 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS223."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K., Tiedje J.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS223.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001252 Genomic DNA. Translation: ACK47009.1.
RefSeqYP_002358432.1. NC_011663.1.

3D structure databases

ProteinModelPortalB8EAI0.
SMRB8EAI0. Positions 1-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING407976.Sbal223_2515.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK47009; ACK47009; Sbal223_2515.
GeneID7087051.
KEGGsbp:Sbal223_2515.
PATRIC23481325. VBISheBal125792_2603.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.
ProtClustDBPRK05679.

Enzyme and pathway databases

BioCycSBAL407976:GJ6Y-2605-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_SHEB2
AccessionPrimary (citable) accession number: B8EAI0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 35 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