Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6D5V3 (PDXH_PECAS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:ECA1935
OrganismPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica) [Complete proteome] [HAMAP]
Taxonomic identifier218491 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

Protein attributes

Sequence length227 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 – 227227Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167705

Regions

Nucleotide binding91 – 922FMN By similarity
Nucleotide binding155 – 1562FMN By similarity
Region23 – 264Substrate binding By similarity
Region206 – 2083Substrate binding By similarity

Sites

Binding site761FMN By similarity
Binding site791FMN; via amide nitrogen By similarity
Binding site811Substrate By similarity
Binding site981FMN By similarity
Binding site1381Substrate By similarity
Binding site1421Substrate By similarity
Binding site1461Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6D5V3 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: E39BF5D3EAA573D3

FASTA22726,398
        10         20         30         40         50         60 
MTQERSPSDG TPLIQPADIA DIRREYTRGG LRRGDLPANP LDLFERWLKQ ACEAKLADPT 

        70         80         90        100        110        120 
AMSVATVDER GQPYQRIVLL KHYDEKGMVF YTNMGSRKAH HLENNPRISL LFPWHVLERQ 

       130        140        150        160        170        180 
VMVLGRVEKL PALEVLKYFH SRPKDSQIGA WVSKQSSRIS ARGVLESKFL ELKQKFQNGE 

       190        200        210        220 
VPLPSFWGGF RVVIDSVEFW QGGEHRLHDR FFYQRQEENW QIDRLAP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950851 Genomic DNA. Translation: CAG74838.1.
RefSeqYP_050032.1. NC_004547.2.

3D structure databases

ProteinModelPortalQ6D5V3.
SMRQ6D5V3. Positions 19-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218491.ECA1935.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG74838; CAG74838; ECA1935.
GeneID2882128.
KEGGeca:ECA1935.
PATRIC20479164. VBIPecAtr54885_1968.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANMGSRKA.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycPATR218491:GJNB-1976-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_PECAS
AccessionPrimary (citable) accession number: Q6D5V3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: August 16, 2004
Last modified: May 14, 2014
This is version 73 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