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UniProtKB/Swiss-Prot entry Q8G2A9

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

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Entry information
Entry name PDXH_BRUSU
Primary accession number Q8G2A9
Secondary accession numbers None
Integrated into Swiss-Prot on January 24, 2006
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 39)
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: BR0416
From
Brucella suis [TaxID: 29461] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Brucellaceae; Brucella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1330 / Biovar 1;
DOI=10.1073/pnas.192319099; PubMed=12271122 [NCBI, ExPASy, EBI, Israel, Japan]
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts.";
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
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
AE014291; AAN29361.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR AG3441; AG3441.
RefSeq NP_697446.1; -.
3D structure databases
HSSP P28225; 1DNL. [HSSP ENTRY / PDB]
ModBase Q8G2A9.
Enzyme and pathway databases
BioCyc BSUI204722:BR_0416-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).
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.
Genome annotation databases
GeneID 1166077; -.
GenomeReviews AE014291_GR; BR0416.
KEGG bms:BR0416; -.
TIGR BR0416; -.
Phylogenomic databases
HOGENOM Q8G2A9; -.
Other
ProtoNet Q8G2A9.
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   208  208     Pyridoxine/pyridoxamine 5'-phosphate oxidase. PRO_0000167694
NP_BIND   70    71  2     FMN (By similarity). 
NP_BIND   134   135  2     FMN (By similarity). 
REGION   185   187  3     Substrate binding (By similarity). 
BINDING   55    55        FMN (By similarity). 
BINDING   58    58        FMN; via amide nitrogen (By similarity). 
BINDING   60    60        Substrate (By similarity). 
BINDING   77    77        FMN (By similarity). 
BINDING   117   117        Substrate (By similarity). 
BINDING   121   121        Substrate (By similarity). 
BINDING   125   125        Substrate (By similarity). 
Sequence information
Length: 208 AA [This is the length of the unprocessed precursor] Molecular weight: 23866 Da [This is the MW of the unprocessed precursor] CRC64: CB1F50BC9612DE28 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MEPVKMTNSS DDFTQSAEPF KLFAEWLADA AKSEPNDPNA VALATVDPDG LPNVRMVLLK 

        70         80         90        100        110        120 
DFDETGFVFY TNYESKKGQE ILSAEKAAMC FHWKSLRRQV RVRGPVEKVS DAEADAYYAS 

       130        140        150        160        170        180 
RPRGSRIGAW ASKQSRPLES RFALEKAVAE YTAKYAIGDI PRPPYWSGFR IRPVSIEFWH 

       190        200 
DRPFRLHDRV LFTRPTPEGD WNKDRLYP
Q8G2A9 in FASTA format

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