XYOA_STRCO
ID XYOA_STRCO Reviewed; 418 AA.
AC Q9ZBU1;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Alditol oxidase {ECO:0000303|PubMed:17517896, ECO:0000303|PubMed:18154360};
DE Short=AldO {ECO:0000303|PubMed:17517896, ECO:0000303|PubMed:18154360};
DE EC=1.1.3.41 {ECO:0000269|PubMed:17517896};
DE AltName: Full=Xylitol oxidase {ECO:0000305|PubMed:17517896};
GN Name=xyoA; Synonyms=aldo {ECO:0000303|PubMed:17517896};
GN OrderedLocusNames=SCO6147; ORFNames=SC1A9.11c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF HIS-46.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=17517896; DOI=10.1074/jbc.m610849200;
RA Heuts D.P., van Hellemond E.W., Janssen D.B., Fraaije M.W.;
RT "Discovery, characterization, and kinetic analysis of an alditol oxidase
RT from Streptomyces coelicolor.";
RL J. Biol. Chem. 282:20283-20291(2007).
RN [3] {ECO:0007744|PDB:2VFR, ECO:0007744|PDB:2VFS, ECO:0007744|PDB:2VFT, ECO:0007744|PDB:2VFU, ECO:0007744|PDB:2VFV}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEXES WITH D-SORBITOL;
RP D-MANNITOL; XYLITOL AND FAD.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=18154360; DOI=10.1021/bi701886t;
RA Forneris F., Heuts D.P., Delvecchio M., Rovida S., Fraaije M.W.,
RA Mattevi A.;
RT "Structural analysis of the catalytic mechanism and stereoselectivity in
RT Streptomyces coelicolor alditol oxidase.";
RL Biochemistry 47:978-985(2008).
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 a poor
CC efficiency with D-mannitol and L-threitol.
CC {ECO:0000269|PubMed:17517896}.
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:17517896};
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:17517896};
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:0000305|PubMed:17517896};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17517896, ECO:0000269|PubMed:18154360};
CC Note=Binds 1 FAD covalently per subunit. {ECO:0000269|PubMed:17517896,
CC ECO:0000269|PubMed:18154360};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 mM for xylitol {ECO:0000269|PubMed:17517896};
CC KM=1.4 mM for D-sorbitol {ECO:0000269|PubMed:17517896};
CC KM=36 mM for D-mannitol {ECO:0000269|PubMed:17517896};
CC KM=25 mM for L-threitol {ECO:0000269|PubMed:17517896};
CC Note=kcat is 13 sec(-1) with xylitol as substrate. kcat is 17 sec(-1)
CC with D-sorbitol as substrate. kcat is 9.2 sec(-1) with D-mannitol as
CC substrate. kcat is 6.3 sec(-1) with L-threitol as substrate.
CC {ECO:0000269|PubMed:17517896};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17517896}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AL939126; CAA22381.1; -; Genomic_DNA.
DR PIR; T34660; T34660.
DR RefSeq; NP_630252.1; NC_003888.3.
DR RefSeq; WP_011030685.1; NZ_VNID01000009.1.
DR PDB; 2VFR; X-ray; 1.10 A; A=1-418.
DR PDB; 2VFS; X-ray; 1.60 A; A=1-418.
DR PDB; 2VFT; X-ray; 1.60 A; A=1-418.
DR PDB; 2VFU; X-ray; 1.90 A; A=1-418.
DR PDB; 2VFV; X-ray; 1.72 A; A=1-418.
DR PDBsum; 2VFR; -.
DR PDBsum; 2VFS; -.
DR PDBsum; 2VFT; -.
DR PDBsum; 2VFU; -.
DR PDBsum; 2VFV; -.
DR AlphaFoldDB; Q9ZBU1; -.
DR SMR; Q9ZBU1; -.
DR STRING; 100226.SCO6147; -.
DR GeneID; 1101588; -.
DR KEGG; sco:SCO6147; -.
DR PATRIC; fig|100226.15.peg.6251; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_003896_4_2_11; -.
DR InParanoid; Q9ZBU1; -.
DR OMA; HWGKVFT; -.
DR PhylomeDB; Q9ZBU1; -.
DR BRENDA; 1.1.3.41; 5998.
DR EvolutionaryTrace; Q9ZBU1; -.
DR Proteomes; UP000001973; Chromosome.
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:0080049; F:L-gulono-1,4-lactone dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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 3D-structure; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..418
FT /note="Alditol oxidase"
FT /id="PRO_0000128174"
FT DOMAIN 13..179
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 41..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2VFR, ECO:0007744|PDB:2VFS,
FT ECO:0007744|PDB:2VFT, ECO:0007744|PDB:2VFU"
FT BINDING 106
FT /ligand="D-sorbitol"
FT /ligand_id="ChEBI:CHEBI:17924"
FT /evidence="ECO:0007744|PDB:2VFT"
FT BINDING 106
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2VFR, ECO:0007744|PDB:2VFS,
FT ECO:0007744|PDB:2VFT, ECO:0007744|PDB:2VFU"
FT BINDING 106
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0007744|PDB:2VFS"
FT BINDING 111
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2VFR, ECO:0007744|PDB:2VFS,
FT ECO:0007744|PDB:2VFT, ECO:0007744|PDB:2VFU"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2VFR, ECO:0007744|PDB:2VFS,
FT ECO:0007744|PDB:2VFT, ECO:0007744|PDB:2VFU"
FT BINDING 118..121
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2VFR, ECO:0007744|PDB:2VFS,
FT ECO:0007744|PDB:2VFT, ECO:0007744|PDB:2VFU"
FT BINDING 169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2VFR, ECO:0007744|PDB:2VFS,
FT ECO:0007744|PDB:2VFT, ECO:0007744|PDB:2VFU"
FT BINDING 320
FT /ligand="D-sorbitol"
FT /ligand_id="ChEBI:CHEBI:17924"
FT /evidence="ECO:0007744|PDB:2VFT"
FT BINDING 320
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0007744|PDB:2VFS"
FT BINDING 322
FT /ligand="D-sorbitol"
FT /ligand_id="ChEBI:CHEBI:17924"
FT /evidence="ECO:0007744|PDB:2VFT"
FT BINDING 322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2VFR, ECO:0007744|PDB:2VFS,
FT ECO:0007744|PDB:2VFT, ECO:0007744|PDB:2VFU"
FT BINDING 322
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0007744|PDB:2VFS"
FT BINDING 345
FT /ligand="D-sorbitol"
FT /ligand_id="ChEBI:CHEBI:17924"
FT /evidence="ECO:0007744|PDB:2VFT"
FT BINDING 345
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0007744|PDB:2VFS"
FT BINDING 372
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2VFR, ECO:0007744|PDB:2VFS,
FT ECO:0007744|PDB:2VFT, ECO:0007744|PDB:2VFU"
FT BINDING 375
FT /ligand="D-sorbitol"
FT /ligand_id="ChEBI:CHEBI:17924"
FT /evidence="ECO:0007744|PDB:2VFT"
FT BINDING 375
FT /ligand="xylitol"
FT /ligand_id="ChEBI:CHEBI:17151"
FT /evidence="ECO:0007744|PDB:2VFS"
FT MOD_RES 46
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000269|PubMed:18154360,
FT ECO:0000305|PubMed:17517896, ECO:0007744|PDB:2VFR"
FT MUTAGEN 46
FT /note="H->A: Does not contain FAD, and shows no oxidase
FT activity."
FT /evidence="ECO:0000269|PubMed:17517896"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2VFS"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:2VFR"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2VFV"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 216..229
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 298..307
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 316..324
FT /evidence="ECO:0007829|PDB:2VFR"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 350..364
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:2VFR"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:2VFR"
SQ SEQUENCE 418 AA; 44347 MW; 2A80DF7735A87DCD CRC64;
MSDITVTNWA GNITYTAKEL LRPHSLDALR ALVADSARVR VLGSGHSFNE IAEPGDGGVL
LSLAGLPSVV DVDTAARTVR VGGGVRYAEL ARVVHARGLA LPNMASLPHI SVAGSVATGT
HGSGVGNGSL ASVVREVELV TADGSTVVIA RGDERFGGAV TSLGALGVVT SLTLDLEPAY
EMEQHVFTEL PLAGLDPATF ETVMAAAYSV SLFTDWRAPG FRQVWLKRRT DRPLDGFPYA
APAAEKMHPV PGMPAVNCTE QFGVPGPWHE RLPHFRAEFT PSSGAELQSE YLMPREHALA
ALHAMDAIRE TLAPVLQTCE IRTVAADAQW LSPAYGRDTV AAHFTWVEDT AAVLPVVRRL
EEALVPFAAR PHWGKVFTVP AGELRALYPR LADFGALAGA LDPAGKFTNA FVRGVLAG
