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UniProtKB/Swiss-Prot entry Q8FH87

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

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Entry information
Entry name PDXH_ECOL6
Primary accession number Q8FH87
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 44)
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: c2030
From
Escherichia coli O6 [TaxID: 217992] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
DOI=10.1073/pnas.252529799; PubMed=12471157 [NCBI, ExPASy, EBI, Israel, Japan]
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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
AE014075; AAN80490.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_753925.1; -.
3D structure databases
HSSP P28225; 1G79. [HSSP ENTRY / PDB]
SMR Q8FH87; 5-218.
ModBase Q8FH87.
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 1036125; -.
GenomeReviews AE014075_GR; c2030.
KEGG ecc:c2030; -.
Phylogenomic databases
HOGENOM Q8FH87; -.
Genome annotation databases
CMR Q8FH87; c2030.
Other
ProtoNet Q8FH87.
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   218  218     Pyridoxine/pyridoxamine 5'-phosphate oxidase. PRO_0000167708
NP_BIND   82    83  2     FMN (By similarity). 
NP_BIND   146   147  2     FMN (By similarity). 
REGION   14    17  4     Substrate binding (By similarity). 
REGION   197   199  3     Substrate binding (By similarity). 
BINDING   67    67        FMN (By similarity). 
BINDING   70    70        FMN; via amide nitrogen (By similarity). 
BINDING   72    72        Substrate (By similarity). 
BINDING   89    89        FMN (By similarity). 
BINDING   129   129        Substrate (By similarity). 
BINDING   133   133        Substrate (By similarity). 
BINDING   137   137        Substrate (By similarity). 
Sequence information
Length: 218 AA [This is the length of the unprocessed precursor] Molecular weight: 25603 Da [This is the MW of the unprocessed precursor] CRC64: A497CC1388D3EA19 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSDNDELQQI AHLRREYTKG GLRRRDLPAD PLTLFERWLS QACEAKLADP TAMVVATVDE 

        70         80         90        100        110        120 
HDQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS LLFPWHTLER QVMVIGKAER 

       130        140        150        160        170        180 
LSTLEVMKYF HSRPRDSQIG AWVSKQSSRI SARGILESKF LELKQKFQQG EVPLPSFWGG 

       190        200        210 
FRVSLEQIEF WQGGEHRLHD RFLYQRENDA WKIDRLAP
Q8FH87 in FASTA format

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