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UniProtKB/Swiss-Prot entry Q7P203


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

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Entry information
Entry name PDXH_CHRVO
Primary accession number Q7P203
Secondary accession numbers None
Integrated into Swiss-Prot on January 24, 2006
Sequence was last modified on December 15, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 42)
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: CV_0059
From
Chromobacterium violaceum [TaxID: 536] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; Chromobacterium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131;
DOI=10.1073/pnas.1832124100; PubMed=14500782 [NCBI, ExPASy, EBI, Israel, Japan]
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability.";
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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
AE016825; AAQ57738.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_899729.1; -.
3D structure databases
HSSP P28225; 1G79. [HSSP ENTRY / PDB]
ModBase Q7P203.
Enzyme and pathway databases
BioCyc CVIO243365:CV_0059-MON; -.
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).
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 Q7P203.
ProtoNet Q7P203.
Genome annotation databases
GeneID 2550220; -.
GenomeReviews AE016825_GR; CV_0059.
KEGG cvi:CV_0059; -.
NMPDR fig|243365.1.peg.59; -.
Phylogenomic databases
HOGENOM Q7P203; -.
Genome annotation databases
CMR Q7P203; CV_0059.
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   213  213     Pyridoxine/pyridoxamine 5'-phosphate oxidase. PRO_0000167698
NP_BIND   77    78  2     FMN (By similarity). 
NP_BIND   141   142  2     FMN (By similarity). 
REGION   9    12  4     Substrate binding (By similarity). 
REGION   191   193  3     Substrate binding (By similarity). 
BINDING   62    62        FMN (By similarity). 
BINDING   65    65        FMN; via amide nitrogen (By similarity). 
BINDING   67    67        Substrate (By similarity). 
BINDING   84    84        FMN (By similarity). 
BINDING   124   124        Substrate (By similarity). 
BINDING   128   128        Substrate (By similarity). 
BINDING   132   132        Substrate (By similarity). 
Sequence information
Length: 213 AA [This is the length of the unprocessed precursor] Molecular weight: 23831 Da [This is the MW of the unprocessed precursor] CRC64: 8064C66220EB3B8E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLNLADIRL EYSKKELSPE DCLPDAVAQF EIWLNEAIAA QVPEPTAMNL AAIGADGRPS 

        70         80         90        100        110        120 
SRIVLLKGVE DGQLLFYTNY QSRKGQALEA NPYVALNFFW PELERQVRIE GKAARVAPEV 

       130        140        150        160        170        180 
SDAYFASRPY TSRLGAWASE QSREIASKAT LVTRAAMFGA RYPINVPRPP HWGGFAVVPD 

       190        200        210 
RVEFWQGRPS RLHDRVLYTL QPDGGWSRSR LAP 

Q7P203 in FASTA format

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