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A1ULM8 (PDXH_MYCSK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. 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:Mkms_4545
OrganismMycobacterium sp. (strain KMS) [Complete proteome] [HAMAP]
Taxonomic identifier189918 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length220 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 – 220220Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000292307

Regions

Nucleotide binding87 – 882FMN By similarity
Nucleotide binding151 – 1522FMN By similarity
Region13 – 164Substrate binding By similarity
Region203 – 2053Substrate binding By similarity

Sites

Binding site721FMN By similarity
Binding site751FMN; via amide nitrogen By similarity
Binding site771Substrate By similarity
Binding site941FMN By similarity
Binding site1341Substrate By similarity
Binding site1381Substrate By similarity
Binding site1421Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1ULM8 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 7EAA4A8D3577DBE5

FASTA22024,387
        10         20         30         40         50         60 
MKKADNEHLA RMRVEYGSVE KDGSADLDVD WLADGWVALL RRWLADAEAA GIAEPNAIVL 

        70         80         90        100        110        120 
GTVDAGGRPV TRTVLCKSVD DTGITFFTNY GSAKGEDLAS TPYASATFPW FALGRQVHVR 

       130        140        150        160        170        180 
GPVTKVSAEE TADYWSKRPR GSQLGAWASQ QSRPIASRAE LLDQLAEVTE RFADHDTVPV 

       190        200        210        220 
PPDWGGYRIT AEVVEFWQGR ESRVHNRIRV HDGRIERLQP 

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium sp. KMS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KMS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000518 Genomic DNA. Translation: ABL93736.1.
RefSeqYP_940526.1. NC_008705.1.

3D structure databases

ProteinModelPortalA1ULM8.
SMRA1ULM8. Positions 20-220.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189918.Mkms_4545.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL93736; ABL93736; Mkms_4545.
GeneID4612489.
KEGGmkm:Mkms_4545.
PATRIC18108128. VBIMycSp70743_5077.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANFESQKG.
OrthoDBEOG60KN2Z.
ProtClustDBPRK05679.

Enzyme and pathway databases

BioCycMSP189918:GH4X-4588-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_MYCSK
AccessionPrimary (citable) accession number: A1ULM8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: February 6, 2007
Last modified: April 16, 2014
This is version 51 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