ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry A3MHF0

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PDXH_BURM7
Primary accession number A3MHF0
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on April 3, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 17)
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: BMA10247_0107
From
Burkholderia mallei (strain NCTC 10247) [TaxID: 320389] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DeShazer D., Woods D.E., Nierman W.C.;
Submitted (JAN-2007) 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
CP000548; ABO04885.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001079686.1; -.
3D structure databases
ModBase A3MHF0.
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.
ProtoNet A3MHF0.
Genome annotation databases
GeneID 4892035; -.
GenomeReviews CP000548_GR; BMA10247_0107.
KEGG bmn:BMA10247_0107; -.
TIGR BMA10247_0107; -.
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   214  214     Pyridoxine/pyridoxamine 5'-phosphate oxidase. PRO_1000069684
NP_BIND   76    77  2     FMN (By similarity). 
NP_BIND   140   141  2     FMN (By similarity). 
REGION   8    11  4     Substrate binding (By similarity). 
REGION   190   192  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: 214 AA [This is the length of the unprocessed precursor] Molecular weight: 24295 Da [This is the MW of the unprocessed precursor] CRC64: 0BA6365597CAB424 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTTLADLRTN YSRASLDAAD VNPNPFVQFD VWFKEALDAQ LPEPNTMTLA TVDESGRPSA 

        70         80         90        100        110        120 
RIVLIKGADE RGFVFFTNYE SRKGRELAHN PNAALLFYWI ELERQVRVEG RIEKTSEEES 

       130        140        150        160        170        180 
DRYFASRPLG SRIGAWASEQ SAVIESRALL EAREKEIGAR FGENPPRPPH WGGYRLVPSS 

       190        200        210 
IEFWQGRPSR LHDRLLYTRD AASASGWKIT RLAP
A3MHF0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!