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Q3MFQ5 (PDXH_ANAVT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Ava_0557
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena

Protein attributes

Sequence length214 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 MF_01629

Catalytic activity

Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. HAMAP MF_01629

Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2. HAMAP MF_01629

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_01629

Pathway

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. HAMAP MF_01629

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.

Subunit structure

Homodimer By similarity. HAMAP MF_01629

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   LigandFMN
Flavoprotein
   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: InterPro

pyridoxamine-phosphate oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 214214Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629
PRO_0000255850

Regions

Nucleotide binding77 – 782FMN By similarity
Nucleotide binding141 – 1422FMN By similarity
Region9 – 124Substrate binding By similarity
Region192 – 1943Substrate binding By similarity

Sites

Binding site621FMN By similarity
Binding site651FMN; via amide nitrogen By similarity
Binding site671Substrate By similarity
Binding site841FMN By similarity
Binding site1241Substrate By similarity
Binding site1281Substrate By similarity
Binding site1321Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3MFQ5 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 370A98CBBD49CAAE

FASTA21425,160
        10         20         30         40         50         60 
MDRTIADLRK DYTLEALSEV EVDTNPFRQF KRWFEQALAA QLPEPNAMTI ATSTPDGQPS 

        70         80         90        100        110        120 
ARMVLLKDFD ERGFVFFTNY NSRKGQELAE NPQAALVFWW AELERQVRIS GRVEKVSESE 

       130        140        150        160        170        180 
SDYYFYSRPA NSRLGAWVSN QSEIIASREV LEQRMQEFQH KYENQEIPRP SHWGGLRVIP 

       190        200        210 
SQIEFWQGRS SRLHDRLLYT LLNDDSWEIH RLSP

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000117 Genomic DNA. Translation: ABA20181.1.
RefSeqYP_321076.1. NC_007413.1.

3D structure databases

HSSPHSSP built from PDB template 2A2J based on UniProtKB P65682.
ProteinModelPortalQ3MFQ5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3MFQ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3682329.
GenomeReviewsGene locus Ava_0557 in contig CP000117_GR.
KEGGava:Ava_0557.
NMPDRfig|240292.3.peg.2485.
PATRIC35421498. VBIAnaVar43351_1320.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHBG327559.
OMAFTFFTNY.
PhylomeDBQ3MFQ5.
ProtClustDBCLSK895487.

Enzyme and pathway databases

BioCycAVAR240292:AVA_0557-MONOMER.

Family and domain databases

HAMAPMF_01629. PdxH.
[Tree]
InterProIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
IPR009002. Split_barrel_FMN-bd-related.
[Graphical view]
Gene3DG3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit.
KOK00275.
PANTHERPTHR10851. Pyridox_oxidase. 1 hit.
PfamPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMSSF50475. FMN_binding. 1 hit.
TIGRFAMsTIGR00558. PdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_ANAVT
AccessionPrimary (citable) accession number: Q3MFQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 25, 2005
Last modified: January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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