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UniProtKB/Swiss-Prot entry B1IQB6

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

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Entry information
Entry name PDXH_ECOLC
Primary accession number B1IQB6
Secondary accession numbers None
Integrated into Swiss-Prot on May 20, 2008
Sequence was last modified on April 29, 2008 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 7)
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: EcolC_1991
From
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) [TaxID: 481805] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Ingram L., Richardson P.;
"Complete sequence of Escherichia coli C str. ATCC 8739.";
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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
CP000946; ACA77637.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001724964.1; -.
3D structure databases
ModBase B1IQB6.
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.
PROSITE PS01064; PYRIDOX_OXIDASE; 1.
ProtoNet B1IQB6.
Genome annotation databases
GeneID 6068157; -.
GenomeReviews CP000946_GR; EcolC_1991.
KEGG ecl:EcolC_1991; -.
CMR B1IQB6; EcolC_1991.
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   218  218     Pyridoxine/pyridoxamine 5'-phosphate oxidase. PRO_1000088113
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: 25545 Da [This is the MW of the unprocessed precursor] CRC64: 8B47CEEEA6CEF5F9 [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 
HGQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS LLFPWHTLER QVMVIGKAER 

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

       190        200        210 
FRVSLEQIEF WQGGEHRLHD RFLYQRENDA WKIDRLAP
B1IQB6 in FASTA format

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