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Q9KKM4 (PDXH_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 79. 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:VC_A1079
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length211 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167765

Regions

Nucleotide binding75 – 762FMN By similarity
Nucleotide binding139 – 1402FMN By similarity
Region7 – 104Substrate binding By similarity
Region190 – 1923Substrate binding By similarity

Sites

Binding site601FMN By similarity
Binding site631FMN; via amide nitrogen By similarity
Binding site651Substrate By similarity
Binding site821FMN By similarity
Binding site1221Substrate By similarity
Binding site1261Substrate By similarity
Binding site1301Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KKM4 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 27A1B55B0DEE098E

FASTA21124,363
        10         20         30         40         50         60 
MDLSDIRREY IHGGLRRKDL QANPIDQFNL WLQQAIDANL SDPTAMTVAT VDEHGQPFQR 

        70         80         90        100        110        120 
IVLLKNVDDA GFVFYTNLGS RKAQHIAHNN KISLHFPWHP LERQVHITGV AEKLTAMENM 

       130        140        150        160        170        180 
KYFMSRPKES QIAAIASHQS SRISARGVLE GKYLELKQKF ANGEIPVPSF WGGYRIRPES 

       190        200        210 
LEFWQGGEHR LHDRFLYSRQ DDNWTVDRLA P 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003853 Genomic DNA. Translation: AAF96972.1.
PIRC82381.
RefSeqNP_233460.1. NC_002506.1.

3D structure databases

ProteinModelPortalQ9KKM4.
SMRQ9KKM4. Positions 3-211.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VCA1079.

Protocols and materials databases

DNASU2611970.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF96972; AAF96972; VC_A1079.
GeneID2611970.
KEGGvch:VCA1079.
PATRIC20086674. VBIVibCho83274_3684.

Phylogenomic databases

eggNOGCOG0259.
KOK00275.
OMANMGSRKA.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycVCHO:VCA1079-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_VIBCH
AccessionPrimary (citable) accession number: Q9KKM4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 79 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