NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).

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

BA000040; BAC47889.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_769264.1; -.

3D structure databases

HSSP

P28225; 1G79. [HSSP ENTRY / PDB]

ModBase

Q89RY8.

Enzyme and pathway databases

BioCyc

BJAP224911:BLL2624-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.

Genome annotation databases

GeneID

1051429; -.

GenomeReviews

BA000040_GR; bll2624.

KEGG

bja:bll2624; -.

NMPDR

fig|224911.1.peg.2624; -.

Phylogenomic databases

HOGENOM

Q89RY8; -.

Genome annotation databases

CMR

Q89RY8; bll2624.

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`	`1 213`	`213`	`Pyridoxine/pyridoxamine 5'-phosphate oxidase.`	`PRO_0000167692`
`NP_BIND`	`75 76`	`2`	`FMN (By similarity).`
`NP_BIND`	`139 140`	`2`	`FMN (By similarity).`
`REGION`	`190 192`	`3`	`Substrate binding (By similarity).`
`BINDING`	`60 60`		`FMN (By similarity).`
`BINDING`	`63 63`		`FMN; via amide nitrogen (By similarity).`
`BINDING`	`65 65`		`Substrate (By similarity).`
`BINDING`	`82 82`		`FMN (By similarity).`
`BINDING`	`122 122`		`Substrate (By similarity).`
`BINDING`	`126 126`		`Substrate (By similarity).`

Sequence information

Length: 213 AA [This is the length of the unprocessed precursor]

Molecular weight: 24181 Da [This is the MW of the unprocessed precursor]

CRC64: D12CF55C86CFBFB6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTDTTSMKHQ TPLTSGDFTA ADEPFALFET WLNEAIKSEP NDPNAMALAT VDPDGLPDVR 

        70         80         90        100        110        120 
MVLMKGFDTE GFVFYSHIAS QKGRELAANP KAALLFHWKS LRRQVRIRGN VTPVTDAEAD 

       130        140        150        160        170        180 
AYFATRPKQA QIGAWASKQS EALESRFAFE QAIAKVAAKY IIGEVPRPPG WSGWRITPVR 

       190        200        210 
IEFWHDRPFR LHDRIEFRRD AAGQKWSKTR MYP

Q89RY8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
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