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Q2GCC6 (PDXH_NOVAD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. 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:Saro_0048
OrganismNovosphingobium aromaticivorans (strain DSM 12444) [Complete proteome] [HAMAP]
Taxonomic identifier279238 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeNovosphingobium

Protein attributes

Sequence length203 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 – 203203Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000255874

Regions

Nucleotide binding66 – 672FMN By similarity
Nucleotide binding130 – 1312FMN By similarity
Region181 – 1833Substrate binding By similarity

Sites

Binding site511FMN By similarity
Binding site541FMN; via amide nitrogen By similarity
Binding site561Substrate By similarity
Binding site731FMN By similarity
Binding site1131Substrate By similarity
Binding site1171Substrate By similarity
Binding site1211Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2GCC6 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 985D4833105067AC

FASTA20322,750
        10         20         30         40         50         60 
MNSERTAEAI PHADPLSIFE SWFAEARASE PNDPNAMALA TATAEGVPSV RMVLLKGHGP 

        70         80         90        100        110        120 
DGFVFYTNLQ SRKGGELAAN HHVALLFHWK SLRRQIRIEG TIAKVTPAEA DAYFASRHPE 

       130        140        150        160        170        180 
SRLGSAASDQ SRPLPDRQTY LDRVDALRAQ YPDGNVPRPA HWSGYRVTPS AIEFWQDRDF 

       190        200 
RLHERRRFLA DGQGGWTSTL LYP 

« Hide

References

[1]"Complete sequence of Novosphingobium aromaticivorans DSM 12444."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N. expand/collapse author list , Fredrickson J., Balkwill D., Romine M.F., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 12444.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000248 Genomic DNA. Translation: ABD24497.1.
RefSeqYP_495331.1. NC_007794.1.

3D structure databases

ProteinModelPortalQ2GCC6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279238.Saro_0048.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD24497; ABD24497; Saro_0048.
GeneID3917645.
KEGGnar:Saro_0048.
PATRIC22782666. VBINovAro50627_0050.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycNARO279238:GHBU-48-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_NOVAD
AccessionPrimary (citable) accession number: Q2GCC6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 21, 2006
Last modified: April 16, 2014
This is version 60 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