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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of chromosome 1 of Burkholderia sp. 383.";
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) (By similarity).
CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H₂O + O₂ = pyridoxal 5'-phosphate + NH₃ + H₂O₂.
CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O₂ = pyridoxal 5'-phosphate + H₂O₂.
COFACTOR: Binds 1 FMN per subunit (By similarity).
PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1 .
PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1 .
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.

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

CP000151; ABB09494.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_370138.1; -.

3D structure databases

ModBase

Q39DH2.

Enzyme and pathway databases

BioCyc

BSP36773:BCEP18194_A5900-MON; -.

Ontologies

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.

Genome annotation databases

GeneID

3751131; -.

GenomeReviews

CP000151_GR; Bcep18194_A5900.

KEGG

bur:Bcep18194_A5900; -.

NMPDR

fig|269483.3.peg.7378; -.

Phylogenomic databases

HOGENOM

Q39DH2; -.

Genome annotation databases

CMR

Q39DH2; Bcep18194_A5900.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Flavoprotein; FMN; Oxidoreductase; Pyridoxine biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 214`	`214`	`Pyridoxine/pyridoxamine 5'-phosphate oxidase.`	`PRO_0000255859`
`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: 24312 Da [This is the MW of the unprocessed precursor]

CRC64: 301B29752B17D938 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTLADLRIN YSRASLDEAD VAHDPFAQFD RWFKEALAAK LPEPNTMTLA TVGDDGRPSA 

        70         80         90        100        110        120 
RIVLIKGVDE RGFVFFTNYE SRKGRDLAAH PQAALLFYWI ELERQVRIEG RIEKTSAEES 

       130        140        150        160        170        180 
DRYFASRPLG SRIGAWASEQ SAVIDSRATL EAQEQAVSER YGDNPPRPPH WGGYRLVPDS 

       190        200        210 
IEFWQGRPSR LHDRLLYTRD ADTSPSWSIS RLSP

Q39DH2 in FASTA format

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View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools