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UniProtKB/Swiss-Prot entry A5EXX0

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PDXH_DICNV
Primary accession number A5EXX0
Secondary accession numbers None
Integrated into Swiss-Prot on May 20, 2008
Sequence was last modified on June 12, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 16)
Name and origin of the protein
Protein name Pyridoxine/pyridoxamine 5'-phosphate oxidase
Synonyms EC 1.4.3.5
PNP/PMP oxidase
PNPOx
Pyridoxal 5'-phosphate synthase
Gene name
Name: pdxH
OrderedLocusNames: DNO_1023
From
Dichelobacter nodosus (strain VCS1703A) [TaxID: 246195] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales; Cardiobacteriaceae; Dichelobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt1302; PubMed=17468768 [NCBI, ExPASy, EBI, Israel, Japan]
Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T., Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B., Songer J.G., Rood J.I., Paulsen I.T.;
"Genome sequence and identification of candidate vaccine antigens from the animal pathogen Dichelobacter nodosus.";
Nat. Biotechnol. 25:569-575(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000513; ABQ13205.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001209911.1; -.
3D structure databases
ModBase A5EXX0.
Ontologies
GO
GO:0010181; Molecular function: FMN binding (inferred from electronic annotation from HAMAP).
GO:0004733; Molecular function: pyridoxamine-phosphate oxidase activity (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0008615; Biological process: pyridoxine biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_01629; -; 1.
PBIL [Tree]
InterPro IPR011576; PNPOx_rel_FMN_bd_core.
IPR000659; Pyridox_oxidase.
IPR012349; Split_barrel_FMN_bd.
Graphical view of domain structure.
Gene3D G3DSA:2.30.110.10; PNPOx_FMN_bd; 1.
PANTHER PTHR10851; Pyridox_oxidase; 1.
Pfam PF01243; Pyridox_oxidase; 1.
Pfam graphical view of domain structure.
ProDom PD006312; Pyridox_oxidase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00558; pdxH; 1.
PROSITE PS01064; PYRIDOX_OXIDASE; 1.
BLOCKS A5EXX0.
ProtoNet A5EXX0.
Genome annotation databases
GeneID 5122950; -.
GenomeReviews CP000513_GR; DNO_1023.
KEGG dno:DNO_1023; -.
TIGR DNO_1023; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Flavoprotein; FMN; Oxidoreductase; Pyridoxine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   212  212     Pyridoxine/pyridoxamine 5'-phosphate oxidase. PRO_0000335783
NP_BIND   76    77  2     FMN (By similarity). 
NP_BIND   140   141  2     FMN (By similarity). 
REGION   191   193  3     Substrate binding (By similarity). 
BINDING   61    61        FMN (By similarity). 
BINDING   64    64        FMN; via amide nitrogen (By similarity). 
BINDING   66    66        Substrate (By similarity). 
BINDING   83    83        FMN (By similarity). 
BINDING   123   123        Substrate (By similarity). 
BINDING   127   127        Substrate (By similarity). 
BINDING   131   131        Substrate (By similarity). 
Sequence information
Length: 212 AA [This is the length of the unprocessed precursor] Molecular weight: 24570 Da [This is the MW of the unprocessed precursor] CRC64: C8C9F5F3B890DFE5 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDIGSIRHDF TEHPPLLEQD LAADPIEQFA AWFQYAVDSG ISEPNGFVLA TVAADGQPSQ 

        70         80         90        100        110        120 
RSVLLKLFDE EGFVFYTNYS SQKAEEIEKN AQVSMSFPWY ALQRQIHVYG RAEKIPREQS 

       130        140        150        160        170        180 
LAYFLTRPQG SQIGAWASPQ SKIIESRDFL MLKWQNMKAK FHEGKIPLPD FWGGYRVRPH 

       190        200        210 
KIEFWQGQPS RLHDRFLYEK TENGWTVSRR AP
A5EXX0 in FASTA format

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