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B8H292 (PDXH_CAUCN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 42. 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:CCNA_00966
OrganismCaulobacter crescentus (strain NA1000 / CB15N) [Complete proteome] [HAMAP]
Taxonomic identifier565050 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length222 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 – 222222Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_1000186298

Regions

Nucleotide binding86 – 872FMN By similarity
Nucleotide binding150 – 1512FMN By similarity
Region201 – 2033Substrate binding By similarity

Sites

Binding site711FMN By similarity
Binding site741FMN; via amide nitrogen By similarity
Binding site761Substrate By similarity
Binding site931FMN By similarity
Binding site1331Substrate By similarity
Binding site1371Substrate By similarity
Binding site1411Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B8H292 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 8733734B492753FB

FASTA22225,197
        10         20         30         40         50         60 
MSADPTLIPA SPSEDDYVRQ VREATPPPLL SEEDPFALFA EWLEEAGKKE PNDPNAMTVS 

        70         80         90        100        110        120 
TVDADGMPDS RMVLLKDFDA RGFVFYTNTQ SAKGQELNAH PKAALLFHWK SLRRQVRIRG 

       130        140        150        160        170        180 
TVEPVTEAEA DAYFASRARH SQIGAWASDQ SQPLPDRHAL EKRVAEMGLK FGLGKVPRPP 

       190        200        210        220 
HWSGYRITPV TIEFWRDRPF RLHERLVFDR ADGGWTTKRL FP 

« Hide

References

[1]"The genetic basis of laboratory adaptation in Caulobacter crescentus."
Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V., Walunas T.L., Crosson S.
J. Bacteriol. 192:3678-3688(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NA1000 / CB15N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001340 Genomic DNA. Translation: ACL94431.1.
RefSeqYP_002516339.1. NC_011916.1.

3D structure databases

ProteinModelPortalB8H292.
SMRB8H292. Positions 30-211.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190650.CC_0918.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL94431; ACL94431; CCNA_00966.
GeneID7333096.
KEGGccs:CCNA_00966.
PATRIC21306473. VBICauCre52860_0948.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMASIEFWCD.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycCAULONA1000:CCNA_00966-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_CAUCN
AccessionPrimary (citable) accession number: B8H292
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: June 11, 2014
This is version 42 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