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UniProtKB/Swiss-Prot entry A0LR32

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

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Entry information
Entry name PDXH_ACIC1
Primary accession number A0LR32
Secondary accession numbers None
Integrated into Swiss-Prot on June 26, 2007
Sequence was last modified on December 12, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 15)
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: Acel_0116
From
Acidothermus cellulolyticus (strain ATCC 43068 / 11B) [TaxID: 351607] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Frankineae; Acidothermaceae; Acidothermus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.;
"Complete sequence of Acidothermus cellulolyticus 11B.";
Submitted (OCT-2006) 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
CP000481; ABK51892.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_871878.1; -.
3D structure databases
ModBase A0LR32.
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.
Graphical view of domain structure.
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 A0LR32.
ProtoNet A0LR32.
Genome annotation databases
GeneID 4484559; -.
GenomeReviews CP000481_GR; Acel_0116.
KEGG ace:Acel_0116; -.
CMR A0LR32; Acel_0116.
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   224  224     Pyridoxine/pyridoxamine 5'-phosphate oxidase. PRO_0000292281
NP_BIND   83    84  2     FMN (By similarity). 
NP_BIND   148   149  2     FMN (By similarity). 
REGION   200   202  3     Substrate binding (By similarity). 
BINDING   69    69        FMN (By similarity). 
BINDING   72    72        FMN; via amide nitrogen (By similarity). 
BINDING   74    74        Substrate (By similarity). 
BINDING   90    90        FMN (By similarity). 
BINDING   130   130        Substrate (By similarity). 
BINDING   134   134        Substrate (By similarity). 
BINDING   138   138        Substrate (By similarity). 
Sequence information
Length: 224 AA [This is the length of the unprocessed precursor] Molecular weight: 25428 Da [This is the MW of the unprocessed precursor] CRC64: D50A98E36BA4A6B9 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRHGTHTGSN PYAEAYVEVT AGGLAETDLA ADPIEQFRRW LADAIRYNLP EPTAMVVATA 

        70         80         90        100        110        120 
DADGRPSSRH VLLKSVDDGF VFFTNYRSRK GRDLSENPSA SLCFPWFAIG RQVVVLGTVT 

       130        140        150        160        170        180 
KVTREETEEY FASRPRDSQC GAWSSENQSS VVPSRAWLDE RYAEVAQRFA GVEHIPPPPF 

       190        200        210        220 
WGGFRVIPET VEFWQARPAR MHDRLRYRRT ADGERPWIIE RLSP
A0LR32 in FASTA format

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