XYOA_STRSI
ID XYOA_STRSI Reviewed; 415 AA.
AC Q9KX73;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Alditol oxidase {ECO:0000305|PubMed:16232758};
DE EC=1.1.3.41 {ECO:0000269|PubMed:16232758};
DE AltName: Full=Xylitol oxidase {ECO:0000303|PubMed:16232758};
GN Name=xyoA {ECO:0000303|PubMed:16232758};
OS Streptomyces sp. (strain IKD472 / FERM P-14339).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=268810;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-32 AND 226-239,
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND SUBUNIT.
RC STRAIN=IKD472 / FERM P-14339;
RX PubMed=16232758; DOI=10.1016/s1389-1723(00)88958-6;
RA Yamashita M., Omura H., Okamoto E., Furuya Y., Yabuuchi M., Fukahi K.,
RA Murooka Y.;
RT "Isolation, characterization, and molecular cloning of a thermostable
RT xylitol oxidase from Streptomyces sp. IKD472.";
RL J. Biosci. Bioeng. 89:350-360(2000).
CC -!- FUNCTION: Oxidase that performs selective oxidation of the terminal
CC primary hydroxyl group of several alditols, with a reduction of O2 to
CC H2O2. Shows highest activity on xylitol and D-sorbitol, and to a lesser
CC extent, can also use galactitol, D-mannitol, and D-arabitol as
CC substrates in vitro. Is not active on D-glucose, D-xylose, D-galactose,
CC D-mannose, D-fructose, L-sorbose, L-fucose, myoinositol, glycerol,
CC ethyl alcohol, and meso-erythritol. {ECO:0000269|PubMed:16232758}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alditol + O2 = an aldose + H2O2; Xref=Rhea:RHEA:25908,
CC Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15693, ChEBI:CHEBI:16240, ChEBI:CHEBI:17522; EC=1.1.3.41;
CC Evidence={ECO:0000269|PubMed:16232758};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + xylitol = D-xylose + H2O2; Xref=Rhea:RHEA:22308,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17151,
CC ChEBI:CHEBI:53455; EC=1.1.3.41;
CC Evidence={ECO:0000269|PubMed:16232758};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sorbitol + O2 = D-glucose + H2O2; Xref=Rhea:RHEA:69524,
CC ChEBI:CHEBI:4167, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17924; Evidence={ECO:0000269|PubMed:16232758};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:16232758};
CC Note=Binds 1 FAD covalently per subunit. {ECO:0000269|PubMed:16232758};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.68 mM for xylitol {ECO:0000269|PubMed:16232758};
CC KM=3.51 mM for D-sorbitol {ECO:0000269|PubMed:16232758};
CC KM=1.08 mM for galactitol {ECO:0000269|PubMed:16232758};
CC Vmax=29.2 umol/min/mg enzyme with xylitol as substrate
CC {ECO:0000269|PubMed:16232758};
CC Vmax=37.1 umol/min/mg enzyme with D-sorbitol as substrate
CC {ECO:0000269|PubMed:16232758};
CC Vmax=22.7 umol/min/mg enzyme with galactitol as substrate
CC {ECO:0000269|PubMed:16232758};
CC pH dependence:
CC Optimum pH is 7.5. Is stable in the pH range from 5.5 to 10.5.
CC {ECO:0000269|PubMed:16232758};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius. Is stable at temperatures
CC up to 65 degrees Celsius. {ECO:0000269|PubMed:16232758};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16232758}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; D89822; BAA95146.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KX73; -.
DR SMR; Q9KX73; -.
DR KEGG; ag:BAA95146; -.
DR BioCyc; MetaCyc:MON-14456; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050582; F:xylitol oxidase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR007173; ALO_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR010031; FAD_lactone_oxidase.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43762; PTHR43762; 2.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..415
FT /note="Alditol oxidase"
FT /id="PRO_0000128173"
FT DOMAIN 12..179
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 106
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 106
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 111
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 118..121
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 317
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 319
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 342
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 372
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT MOD_RES 46
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
SQ SEQUENCE 415 AA; 44732 MW; A9550A1B779B6816 CRC64;
MSTAVTNWAG NITYTAKEVH RPATAEELAD VVARSAWGAC AGAAGHSFNE IADPGPDGVL
LRLDALPAET DVDTTARTVR VGGGVRYAEL ARVVHAHGLA LPNMASLPHI SVAGSVATGT
HGSGVTNGPL AAPVREVELV TADGSQVRIA PGERRFGGAV TSLGALGVVT ALTLDLEPAF
EVGQHLFTEL PLRGLDFETV AAAGYSVSLF TDWREPGFRQ VWLKRRTDQE LPDFPWARPA
TVALHPVPGM PAENCTQQFG VPGPWHERLP HFRAEFTPSS GAELQSEYLL PRAHALDALD
AVDRIRDTVA PVLQTCEVRT VAPDEQWLGP SHGRDTVALH FTWVKDTEAV LPVVRRLEEA
LDAFDPRPHW GKVFTTSAAA LRARYPRLAD FRALARELDP SGKFTNTFLR DLLDG
