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 Q3MFQ5

[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_ANAVT
Primary accession number Q3MFQ5
Secondary accession numbers None
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on October 25, 2005 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 24)
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: Ava_0557
From
Anabaena variabilis (strain ATCC 29413 / PCC 7937) [TaxID: 240292] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
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 T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
"Complete sequence of Anabaena variabilis ATCC 29413.";
Submitted (SEP-2005) 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
CP000117; ABA20181.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_321076.1; -.
3D structure databases
ModBase Q3MFQ5.
Enzyme and pathway databases
BioCyc AVAR240292:AVA_0557-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 Q3MFQ5.
ProtoNet Q3MFQ5.
Genome annotation databases
GeneID 3682329; -.
GenomeReviews CP000117_GR; Ava_0557.
KEGG ava:Ava_0557; -.
NMPDR fig|240292.3.peg.2485; -.
Phylogenomic databases
HOGENOM Q3MFQ5; -.
Genome annotation databases
CMR Q3MFQ5; Ava_0557.
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_0000255850
NP_BIND   77    78  2     FMN (By similarity). 
NP_BIND   141   142  2     FMN (By similarity). 
REGION   9    12  4     Substrate binding (By similarity). 
REGION   192   194  3     Substrate binding (By similarity). 
BINDING   62    62        FMN (By similarity). 
BINDING   65    65        FMN; via amide nitrogen (By similarity). 
BINDING   67    67        Substrate (By similarity). 
BINDING   84    84        FMN (By similarity). 
BINDING   124   124        Substrate (By similarity). 
BINDING   128   128        Substrate (By similarity). 
BINDING   132   132        Substrate (By similarity). 
Sequence information
Length: 214 AA [This is the length of the unprocessed precursor] Molecular weight: 25160 Da [This is the MW of the unprocessed precursor] CRC64: 370A98CBBD49CAAE [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDRTIADLRK DYTLEALSEV EVDTNPFRQF KRWFEQALAA QLPEPNAMTI ATSTPDGQPS 

        70         80         90        100        110        120 
ARMVLLKDFD ERGFVFFTNY NSRKGQELAE NPQAALVFWW AELERQVRIS GRVEKVSESE 

       130        140        150        160        170        180 
SDYYFYSRPA NSRLGAWVSN QSEIIASREV LEQRMQEFQH KYENQEIPRP SHWGGLRVIP 

       190        200        210 
SQIEFWQGRS SRLHDRLLYT LLNDDSWEIH RLSP
Q3MFQ5 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!