NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-32 AND 226-239, AND CHARACTERIZATION.
DOI=10.1016/S1389-1723(00)88958-6; PubMed=16232758 [NCBI, ExPASy, EBI, Israel, Japan]
Yamashita M., Omura H., Okamoto E., Furuya Y., Yabuuchi M., Fukahi K., Murooka Y.;
"Isolation, characterization, and molecular cloning of a thermostable xylitol oxidase from Streptomyces sp. IKD472.";
J. Biosci. Bioeng. 89:350-360(2000).

Comments

FUNCTION: Catalyzes the oxidation of xylitol to xylose, also acts on D-sorbitol.
CATALYTIC ACTIVITY: Xylitol + O₂ = xylose + H₂O₂.
COFACTOR: FAD.
SUBUNIT: Monomer (Probable).
SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
SIMILARITY: Contains 1 FAD-binding PCMH-type domain.

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

D89822; BAA95146.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q9KX73.

Ontologies

GO:0050582;	Molecular function: xylitol oxidase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR016168; FAD-linked_Oxase_FAD-bd_sub2.
IPR006094; Oxid_FAD_bind_N.
IPR006093; Oxy_OxRdtase_FAD_BS.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.465.20; FAD-linked_oxidase_FAD-bd_sub2; 1.

Pfam

PF01565; FAD_binding_4; 1.
Pfam graphical view of domain structure.

PROSITE

PS51387; FAD_PCMH; 1.
PS00862; OX2_COVAL_FAD; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 415`	`415`	`Xylitol oxidase.`	`PRO_0000128173`
`DOMAIN`	`12 179`	`168`	`FAD-binding PCMH-type.`
`MOD_RES`	`46 46`		`Tele-8alpha-FAD histidine (By similarity).`

Sequence information

Length: 415 AA [This is the length of the unprocessed precursor]

Molecular weight: 44732 Da [This is the MW of the unprocessed precursor]

CRC64: A9550A1B779B6816 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTAVTNWAG NITYTAKEVH RPATAEELAD VVARSAWGAC AGAAGHSFNE IADPGPDGVL 

        70         80         90        100        110        120 
LRLDALPAET DVDTTARTVR VGGGVRYAEL ARVVHAHGLA LPNMASLPHI SVAGSVATGT 

       130        140        150        160        170        180 
HGSGVTNGPL AAPVREVELV TADGSQVRIA PGERRFGGAV TSLGALGVVT ALTLDLEPAF 

       190        200        210        220        230        240 
EVGQHLFTEL PLRGLDFETV AAAGYSVSLF TDWREPGFRQ VWLKRRTDQE LPDFPWARPA 

       250        260        270        280        290        300 
TVALHPVPGM PAENCTQQFG VPGPWHERLP HFRAEFTPSS GAELQSEYLL PRAHALDALD 

       310        320        330        340        350        360 
AVDRIRDTVA PVLQTCEVRT VAPDEQWLGP SHGRDTVALH FTWVKDTEAV LPVVRRLEEA 

       370        380        390        400        410 
LDAFDPRPHW GKVFTTSAAA LRARYPRLAD FRALARELDP SGKFTNTFLR DLLDG

Q9KX73 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