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UniProtKB/Swiss-Prot entry Q6G4D7

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

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Entry information
Entry name PDXH_BARHE
Primary accession number Q6G4D7
Secondary accession numbers None
Integrated into Swiss-Prot on January 24, 2006
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 34)
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: BH04290
From
Bartonella henselae (Rochalimaea henselae) [TaxID: 38323] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bartonellaceae; Bartonella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49882 / Houston 1;
DOI=10.1073/pnas.0305659101; PubMed=15210978 [NCBI, ExPASy, EBI, Israel, Japan]
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.;
"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae.";
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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
BX897699; CAF27238.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_033267.1; -.
3D structure databases
ModBase Q6G4D7.
Enzyme and pathway databases
BioCyc BHEN283166:BH04290-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 Q6G4D7.
ProtoNet Q6G4D7.
Genome annotation databases
GeneID 2865013; -.
GenomeReviews BX897699_GR; BH04290.
KEGG bhe:BH04290; -.
NMPDR fig|283166.1.peg.395; -.
Phylogenomic databases
HOGENOM Q6G4D7; -.
Genome annotation databases
CMR Q6G4D7; BH04290.
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   207  207     Pyridoxine/pyridoxamine 5'-phosphate oxidase. PRO_0000167684
NP_BIND   68    69  2     FMN (By similarity). 
NP_BIND   132   133  2     FMN (By similarity). 
REGION   183   185  3     Substrate binding (By similarity). 
BINDING   53    53        FMN (By similarity). 
BINDING   56    56        FMN; via amide nitrogen (By similarity). 
BINDING   58    58        Substrate (By similarity). 
BINDING   75    75        FMN (By similarity). 
BINDING   115   115        Substrate (By similarity). 
BINDING   119   119        Substrate (By similarity). 
BINDING   123   123        Substrate (By similarity). 
Sequence information
Length: 207 AA [This is the length of the unprocessed precursor] Molecular weight: 24271 Da [This is the MW of the unprocessed precursor] CRC64: 7702729BA8E64A47 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGNTVQTDND FMQMQKPFAL FAKWLEEATV SEINDPNAMA LATVDKTGFP NVRMVLLKDF 

        70         80         90        100        110        120 
SPQGFVFYTN YESPKGQEIL KSMKASLVFH WKSLRRQVRI RGIVEKVTPQ EADAYFQSRP 

       130        140        150        160        170        180 
RDSRIGAWAS KQSQPLESRF VLEKAIARYT TRYAVGNIPR PPYWSGFRVK PLSIEFWCDR 

       190        200 
PFRLHDRLLF TRDSVEHVDW KRQKLYP
Q6G4D7 in FASTA format

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