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Q487G8 (PDXH_COLP3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:CPS_1053
OrganismColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]
Taxonomic identifier167879 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia

Protein attributes

Sequence length217 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_processpyridoxal phosphate biosynthetic process

Inferred from electronic annotation. Source: GOC

pyridoxine 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 – 217217Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167699

Regions

Nucleotide binding81 – 822FMN By similarity
Nucleotide binding145 – 1462FMN By similarity
Region196 – 1983Substrate binding By similarity

Sites

Binding site661FMN By similarity
Binding site691FMN; via amide nitrogen By similarity
Binding site711Substrate By similarity
Binding site881FMN By similarity
Binding site1281Substrate By similarity
Binding site1321Substrate By similarity
Binding site1361Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q487G8 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 34BCDD1E98C24F38

FASTA21725,231
        10         20         30         40         50         60 
MTLFEKLRCL FTFGQGVALP LPELSSNTTP DQIFEQWFAD ANKSGILLPE AMSVSSCNSD 

        70         80         90        100        110        120 
GQPSSRMVLL KDYDKEGFVF FTNYESRKSH ELAENNKVAL LFHWNVLQRQ IRIEGTVEKV 

       130        140        150        160        170        180 
SIQESADYFH SRDRGSQVGA WASKQSQKLK YDDELKERMS HYQDKFSEGE VPHPEFWGGW 

       190        200        210 
RVKPHAIEFW QGRANRLHDR LCFEKDGETW LNHKLNP 

« Hide

References

[1]"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses."
Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. expand/collapse author list , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 34H / ATCC BAA-681.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000083 Genomic DNA. Translation: AAZ28207.1.
RefSeqYP_267797.1. NC_003910.7.

3D structure databases

ProteinModelPortalQ487G8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167879.CPS_1053.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ28207; AAZ28207; CPS_1053.
GeneID3522466.
KEGGcps:CPS_1053.
PATRIC21465381. VBIColPsy94388_0943.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANFESQKG.
OrthoDBEOG60KN2Z.
ProtClustDBCLSK768225.

Enzyme and pathway databases

BioCycCPSY167879:GI48-1053-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_COLP3
AccessionPrimary (citable) accession number: Q487G8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 61 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