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Q8P6X5 (PDXH_XANCP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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:XCC2840
OrganismXanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]
Taxonomic identifier190485 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length199 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
Reference 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 – 199199Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167773

Regions

Nucleotide binding59 – 602FMN By similarity
Nucleotide binding126 – 1272FMN By similarity
Region177 – 1793Substrate binding By similarity

Sites

Binding site441FMN By similarity
Binding site471FMN; via amide nitrogen By similarity
Binding site491Substrate By similarity
Binding site661FMN By similarity
Binding site1091Substrate By similarity
Binding site1131Substrate By similarity
Binding site1171Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8P6X5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 40E7B36B7C21081D

FASTA19922,275
        10         20         30         40         50         60 
MTDLYAEALA TFATLYAEAQ NSAEIEASAM TVATANLDGR PSARTVLLKA FDARGFVFYT 

        70         80         90        100        110        120 
HLDSAKGRDL QTHPQAALLF LWRSLREAGI QVRIEGGVQL VSADESDAYF ASRPRMSQIG 

       130        140        150        160        170        180 
AWASLQSQTL GSREEFEAAI AKVEATFDGR DVPRPDGWGG FRVVPQAFEF WYGAKFRLHE 

       190 
RWRYEADAAS HWSKRMLYP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008922 Genomic DNA. Translation: AAM42112.1.
RefSeqNP_638188.1. NC_003902.1.

3D structure databases

ProteinModelPortalQ8P6X5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190485.XCC2840.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM42112; AAM42112; XCC2840.
GeneID999790.
KEGGxcc:XCC2840.
PATRIC24076700. VBIXanCam115730_3039.

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANMGSRKA.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycXCAM190485:GIXZ-2838-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_XANCP
AccessionPrimary (citable) accession number: Q8P6X5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 80 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