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O33065 (PDXH_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. 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:ML2131
ORF Names:MLCB57.46
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length219 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.

Sequence caution

The sequence CAC31086.1 differs from that shown. Reason: Erroneous initiation.

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 – 219219Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167721

Regions

Nucleotide binding86 – 872FMN By similarity
Nucleotide binding150 – 1512FMN By similarity
Region13 – 164Substrate binding By similarity
Region202 – 2043Substrate 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
O33065 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 779F8E704AED543C

FASTA21924,388
        10         20         30         40         50         60 
MAGPDDQHLS GMRVEYGSVE KDGSPDLDTD WLYDGWLTLF CKWIDDAERA GVAEPNAMVL 

        70         80         90        100        110        120 
ATVANGRPVS RSVLCKGADE AGIIFFTNYD SDKGDDLAAT PYASVTFPWY QLGRQVHIRG 

       130        140        150        160        170        180 
PVSTVDPQVS EDYWSKRPRG SQLGAWASHQ SRPIASRTAL LDQLLEVTVR FADSELIPLP 

       190        200        210 
PNWGGYLIVP EVVEFWQGRE NRVHNRIRVT GGCIERLQP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z99494 Genomic DNA. Translation: CAB16686.1.
AL583924 Genomic DNA. Translation: CAC31086.1. Different initiation.
PIRF87175.
T45352.
RefSeqNP_302406.2. NC_002677.1.

3D structure databases

ProteinModelPortalO33065.
SMRO33065. Positions 20-219.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML2131.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC31086; CAC31086; CAC31086.
GeneID908903.
KEGGmle:ML2131.
PATRIC18058211. VBIMycLep78757_4028.

Organism-specific databases

LepromaML2131.
CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OrthoDBEOG60KN2Z.
ProtClustDBPRK05679.

Enzyme and pathway databases

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_MYCLE
AccessionPrimary (citable) accession number: O33065
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 95 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