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Q83D18 (PDXH_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:CBU_0928
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length196 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 – 196196Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167700

Regions

Nucleotide binding61 – 622FMN By similarity
Nucleotide binding125 – 1262FMN By similarity
Region175 – 1773Substrate binding By similarity

Sites

Binding site461FMN By similarity
Binding site491FMN; via amide nitrogen By similarity
Binding site511Substrate By similarity
Binding site681FMN By similarity
Binding site1081Substrate By similarity
Binding site1121Substrate By similarity
Binding site1161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83D18 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 75DDC0F2C706C1DA

FASTA19623,636
        10         20         30         40         50         60 
MFRLDLLSDP LEQFKLWYDE AIRHETLHPD AMVLATADSK GKPSARNVLY KGISKGGFLI 

        70         80         90        100        110        120 
FTNYHSRKAH ELDENPQAAW VFYWPKTYKQ VRGEGRVERL TQEESEAYFE TRSYESQIAA 

       130        140        150        160        170        180 
WVSEQSQEIP DREYLITRYK KYREKFQDDV RCPEFWGGFR LIPDRMEFWV GQEHRLHDRF 

       190 
CYLKENQEWK IIRLAP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016828 Genomic DNA. Translation: AAO90455.1.
RefSeqNP_819941.1. NC_002971.3.

3D structure databases

ProteinModelPortalQ83D18.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227377.CBU_0928.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO90455; AAO90455; CBU_0928.
GeneID1208821.
KEGGcbu:CBU_0928.
PATRIC17930563. VBICoxBur82552_0918.

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANMGSRKA.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-919-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_COXBU
AccessionPrimary (citable) accession number: Q83D18
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 76 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

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names