NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=9-941 / Biovar 1;
DOI=10.1128/JB.187.8.2715-2726.2005; PubMed=15805518 [NCBI, ExPASy, EBI, Israel, Japan]
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis.";
J. Bacteriol. 187:2715-2726(2005).

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

AE017223; AAX73835.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_221196.1; -.

3D structure databases

ModBase

Q57EU9.

Enzyme and pathway databases

BioCyc

BABO262698:BRUAB1_0439-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).
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

Q57EU9.

Genome annotation databases

GeneID

3339404; -.

GenomeReviews

AE017223_GR; BruAb1_0439.

KEGG

bmb:BruAb1_0439; -.

Phylogenomic databases

HOGENOM

Q57EU9; -.

Genome annotation databases

CMR

Q57EU9; BruAb1_0439.

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`	`1 208`	`208`	`Pyridoxine/pyridoxamine 5'-phosphate oxidase.`	`PRO_0000255855`
`NP_BIND`	`70 71`	`2`	`FMN (By similarity).`
`NP_BIND`	`134 135`	`2`	`FMN (By similarity).`
`REGION`	`185 187`	`3`	`Substrate binding (By similarity).`
`BINDING`	`55 55`		`FMN (By similarity).`
`BINDING`	`58 58`		`FMN; via amide nitrogen (By similarity).`
`BINDING`	`60 60`		`Substrate (By similarity).`
`BINDING`	`77 77`		`FMN (By similarity).`
`BINDING`	`117 117`		`Substrate (By similarity).`
`BINDING`	`121 121`		`Substrate (By similarity).`
`BINDING`	`125 125`		`Substrate (By similarity).`

Sequence information

Length: 208 AA [This is the length of the unprocessed precursor]

Molecular weight: 23866 Da [This is the MW of the unprocessed precursor]

CRC64: CB1F50BC9612DE28 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEPVKMTNSS DDFTQSAEPF KLFAEWLADA AKSEPNDPNA VALATVDPDG LPNVRMVLLK 

        70         80         90        100        110        120 
DFDETGFVFY TNYESKKGQE ILSAEKAAMC FHWKSLRRQV RVRGPVEKVS DAEADAYYAS 

       130        140        150        160        170        180 
RPRGSRIGAW ASKQSRPLES RFALEKAVAE YTAKYAIGDI PRPPYWSGFR IRPVSIEFWH 

       190        200 
DRPFRLHDRV LFTRPTPEGD WNKDRLYP

Q57EU9 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 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