XYLO_MYCTT
ID XYLO_MYCTT Reviewed; 497 AA.
AC G2QG48;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Xylooligosaccharide oxidase {ECO:0000303|PubMed:27629413};
DE Short=XOS;
DE EC=1.1.3.- {ECO:0000305|PubMed:27629413};
DE Flags: Precursor;
GN Name=xylO {ECO:0000303|PubMed:27629413}; ORFNames=MYCTH_102971;
OS Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS (Sporotrichum thermophile).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX NCBI_TaxID=573729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799;
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
RN [2] {ECO:0007744|PDB:5K8E, ECO:0007744|PDB:5L6F, ECO:0007744|PDB:5L6G}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH FAD AND SUBSTRATES,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-117; ASN-192; ASN-233; ASN-245 AND
RP ASN-289, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27629413; DOI=10.1074/jbc.m116.741173;
RA Ferrari A.R., Rozeboom H.J., Dobruchowska J.M., van Leeuwen S.S.,
RA Vugts A.S., Koetsier M.J., Visser J., Fraaije M.W.;
RT "Discovery of a xylooligosaccharide oxidase from Myceliophthora thermophila
RT C1.";
RL J. Biol. Chem. 291:23709-23718(2016).
CC -!- FUNCTION: Catalyzes the selective oxidation of C1 hydroxyl moieties on
CC mono-, oligo- and polysaccharides with concomitant reduction of
CC molecular oxygen to hydrogen peroxide. This results in the formation of
CC the corresponding lactones, which typically undergo spontaneous
CC hydrolysis. Xylooligosaccharide oxidase is able to oxidize a variety of
CC substrates including D-xylose, D-cellobiose, lactose and arabinose. The
CC enzyme acts primarily on xylooligosaccharides, indicating that it
CC prefers pentose-based oligosaccharides over hexose-based
CC oligosaccharides. {ECO:0000269|PubMed:27629413}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylobiose + O2 = D-xylobiono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59632, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:28309, ChEBI:CHEBI:143156;
CC Evidence={ECO:0000269|PubMed:27629413};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylotriose + O2 = D-xylotriono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59636, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:62783, ChEBI:CHEBI:143164;
CC Evidence={ECO:0000269|PubMed:27629413};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylotetraose + O2 = D-xylotetraono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59640, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:62972, ChEBI:CHEBI:143165;
CC Evidence={ECO:0000269|PubMed:27629413};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:27629413};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000269|PubMed:27629413};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for oxygen {ECO:0000269|PubMed:27629413};
CC KM=342 mM for cellobiose {ECO:0000269|PubMed:27629413};
CC KM=532 mM for lactose {ECO:0000269|PubMed:27629413};
CC KM=359 mM for xylose {ECO:0000269|PubMed:27629413};
CC KM=1.15 mM for xylobiose {ECO:0000269|PubMed:27629413};
CC KM=0.69 mM for xylotriose {ECO:0000269|PubMed:27629413};
CC KM=0.43 mM for xylotetraose {ECO:0000269|PubMed:27629413};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:27629413};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. Stable up to 60 degrees
CC Celsius. {ECO:0000269|PubMed:27629413};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27629413}.
CC -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC N1-histidyl FAD linkage. {ECO:0000269|PubMed:27629413}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; CP003005; AEO58513.1; -; Genomic_DNA.
DR RefSeq; XP_003663758.1; XM_003663710.1.
DR PDB; 5K8E; X-ray; 1.93 A; A=1-497.
DR PDB; 5L6F; X-ray; 1.80 A; A=1-497.
DR PDB; 5L6G; X-ray; 1.79 A; A=1-497.
DR PDBsum; 5K8E; -.
DR PDBsum; 5L6F; -.
DR PDBsum; 5L6G; -.
DR AlphaFoldDB; G2QG48; -.
DR SMR; G2QG48; -.
DR STRING; 573729.G2QG48; -.
DR iPTMnet; G2QG48; -.
DR EnsemblFungi; AEO58513; AEO58513; MYCTH_102971.
DR GeneID; 11510048; -.
DR KEGG; mtm:MYCTH_102971; -.
DR VEuPathDB; FungiDB:MYCTH_102971; -.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_10_1_1; -.
DR InParanoid; G2QG48; -.
DR OrthoDB; 1049549at2759; -.
DR Proteomes; UP000007322; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW Nucleotide-binding; Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..497
FT /note="Xylooligosaccharide oxidase"
FT /id="PRO_5003436280"
FT DOMAIN 57..230
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27629413"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27629413"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27629413"
FT BINDING 451
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27629413"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27629413,
FT ECO:0007744|PDB:5K8E, ECO:0007744|PDB:5L6F,
FT ECO:0007744|PDB:5L6G"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27629413,
FT ECO:0007744|PDB:5K8E, ECO:0007744|PDB:5L6F,
FT ECO:0007744|PDB:5L6G"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27629413,
FT ECO:0007744|PDB:5K8E, ECO:0007744|PDB:5L6F,
FT ECO:0007744|PDB:5L6G"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27629413,
FT ECO:0007744|PDB:5K8E, ECO:0007744|PDB:5L6F,
FT ECO:0007744|PDB:5L6G"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27629413,
FT ECO:0007744|PDB:5K8E, ECO:0007744|PDB:5L6F,
FT ECO:0007744|PDB:5L6G"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 30..79
FT /evidence="ECO:0000269|PubMed:27629413,
FT ECO:0007744|PDB:5K8E, ECO:0007744|PDB:5L6F,
FT ECO:0007744|PDB:5L6G"
FT CROSSLNK 94..155
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000269|PubMed:27629413"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5L6G"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 246..261
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 280..288
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 290..304
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 340..349
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 354..366
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 372..381
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:5L6G"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:5L6G"
FT STRAND 409..420
FT /evidence="ECO:0007829|PDB:5L6G"
FT TURN 423..426
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 427..437
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 458..466
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:5L6G"
FT HELIX 470..480
FT /evidence="ECO:0007829|PDB:5L6G"
SQ SEQUENCE 497 AA; 54324 MW; 03B3D62A1B828EAB CRC64;
MHLLPLTVSA TAVVSAASSP HAKRAAIDEC LKNAKVPVTA RNSTEWKTDA SPFNDRLPYT
PAAIAKPATV EHIQAAVLCA AEVGVKANPK SGGHSYASFG LGGEDGHLVV ELDRMYNVTL
DPETHIATVQ PGARLGHIAT VLYEEGKRAF SHGTCPGVGV GGHSLHGGFG FSSHSHGLAV
DWITSADVVL ANGSLVTASE TENPDLFWAL RGAGSNFGIV ASFRFKTFAA PPNVTSYEIN
LPWTNSSNVV KGWGALQEWL LNGGMPEEMN MRVLGNAFQT QLQGLYHGNA SALKTAIQPL
LALLDANLSS VQEHDWMEGF RHYAYSGEID ITDPGYDQSE TFYSKSLVTS ALPPDVLERV
AEYWIETANK VRRSWYIIID MYGGPNSAVT RVPPGAGSYA FRDPERHLFL YELYDRSFGP
YPDDGFAFLD GWVHAFTGGL DSSDWGMYIN YADPGLDRAE AQEVYYRQNL DRLRRIKQQL
DPTELFYYPQ AVEPAEV
