GOOX_SARSR
ID GOOX_SARSR Reviewed; 499 AA.
AC Q6PW77;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Glucooligosaccharide oxidase {ECO:0000303|PubMed:1764476};
DE Short=GOOX;
DE EC=1.1.3.- {ECO:0000305|PubMed:16332885};
DE Flags: Precursor;
GN Name=gluO;
OS Sarocladium strictum (Black bundle disease fungus) (Acremonium strictum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Sarocladiaceae; Sarocladium.
OX NCBI_TaxID=5046;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 270-294 AND 300-321,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF HIS-95.
RC STRAIN=T1;
RX PubMed=16332885; DOI=10.1128/aem.71.12.8881-8887.2005;
RA Lee M.H., Lai W.L., Lin S.F., Hsu C.S., Liaw S.H., Tsai Y.C.;
RT "Structural characterization of glucooligosaccharide oxidase from
RT Acremonium strictum.";
RL Appl. Environ. Microbiol. 71:8881-8887(2005).
RN [2]
RP PROTEIN SEQUENCE OF 26-55, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=T1;
RX PubMed=1764476; DOI=10.1016/0167-4838(91)90439-7;
RA Lin S.F., Yang T.Y., Inukai T., Yamasaki M., Tsai Y.C.;
RT "Purification and characterization of a novel glucooligosaccharide oxidase
RT from Acremonium strictum T1.";
RL Biochim. Biophys. Acta 1118:41-47(1991).
RN [3] {ECO:0007744|PDB:1ZR6, ECO:0007744|PDB:2AXR}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 26-499 IN COMPLEX WITH PRODUCT
RP ANALOG INHIBITOR AND FAD, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-330 AND
RP ASN-366.
RX PubMed=16154992; DOI=10.1074/jbc.m506078200;
RA Huang C.H., Lai W.L., Lee M.H., Chen C.J., Vasella A., Tsai Y.C.,
RA Liaw S.H.;
RT "Crystal structure of glucooligosaccharide oxidase from Acremonium
RT strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD.";
RL J. Biol. Chem. 280:38831-38838(2005).
RN [4] {ECO:0007744|PDB:3HSU}
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 26-499 IN COMPLEX WITH FAD,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-330 AND ASN-366, AND MUTAGENESIS OF
RP HIS-95 AND CYS-155.
RX PubMed=18768475; DOI=10.1074/jbc.m804331200;
RA Huang C.H., Winkler A., Chen C.L., Lai W.L., Tsai Y.C., Macheroux P.,
RA Liaw S.H.;
RT "Functional roles of the 6-S-cysteinyl, 8alpha-N1-histidyl FAD in
RT glucooligosaccharide oxidase from Acremonium strictum.";
RL J. Biol. Chem. 283:30990-30996(2008).
CC -!- FUNCTION: Catalyzes the selective oxidation of C1 hydroxyl moieties on
CC mono- and disaccharides with concomitant reduction of molecular oxygen
CC to hydrogen peroxide. This results in the formation of the
CC corresponding lactones, which typically undergo spontaneous hydrolysis.
CC Glucooligosaccharide oxidase is able to oxidize the monosaccharide D-
CC glucose as well as the disaccharides maltose, cellobiose, and lactose.
CC In addition, it shows high selectivity for cello- and
CC maltooligosaccharides, indicating that glucooligosaccharide oxidase
CC prefers oligosaccharides with a beta-D-glucosyl unit on the reducing
CC end and additional sugar units linked by alpha- or beta-1,4 glucosidic
CC bonds. {ECO:0000269|PubMed:16332885, ECO:0000269|PubMed:1764476}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-lactose + O2 = H2O2 + lactobiono-1,5-lactone;
CC Xref=Rhea:RHEA:59352, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:36218, ChEBI:CHEBI:143068;
CC Evidence={ECO:0000269|PubMed:16332885};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cellobiose + O2 = D-cellobiono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59316, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17057, ChEBI:CHEBI:17863;
CC Evidence={ECO:0000269|PubMed:16332885};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cellotriose + O2 = D-cellotriono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59656, ChEBI:CHEBI:3528, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:143171;
CC Evidence={ECO:0000269|PubMed:16332885};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cellotetraose + O2 = D-cellotetraono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59660, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:62974, ChEBI:CHEBI:143172;
CC Evidence={ECO:0000269|PubMed:16332885};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cellopentaose + O2 = D-cellopentaono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59664, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:62976, ChEBI:CHEBI:143173;
CC Evidence={ECO:0000269|PubMed:16332885};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cellohexaose + O2 = D-cellohexaono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59668, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:143174, ChEBI:CHEBI:143194;
CC Evidence={ECO:0000269|PubMed:16332885};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:1764476};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000269|PubMed:16154992, ECO:0000269|PubMed:1764476,
CC ECO:0000269|PubMed:18768475};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.12 mM for glucose {ECO:0000269|PubMed:16332885};
CC KM=0.066 mM for lactose {ECO:0000269|PubMed:16332885};
CC KM=2.47 mM for maltose {ECO:0000269|PubMed:16332885};
CC KM=1.11 mM for maltotriose {ECO:0000269|PubMed:16332885};
CC KM=2.51 mM for maltotetraose {ECO:0000269|PubMed:16332885};
CC KM=10.6 mM for maltopentaose {ECO:0000269|PubMed:16332885};
CC KM=2.6 mM for maltohexaose {ECO:0000269|PubMed:16332885};
CC KM=6.95 mM for maltoheptaose {ECO:0000269|PubMed:16332885};
CC KM=0.048 mM for cellobiose {ECO:0000269|PubMed:16332885};
CC KM=0.026 mM for cellotriose {ECO:0000269|PubMed:16332885};
CC KM=0.012 mM for cellotetraose {ECO:0000269|PubMed:16332885};
CC KM=0.026 mM for cellopentaose {ECO:0000269|PubMed:16332885};
CC KM=0.069 mM for cellohexaose {ECO:0000269|PubMed:16332885};
CC pH dependence:
CC Optimum pH is 10. Stable from pH 5 to pH 11.
CC {ECO:0000269|PubMed:1764476};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:1764476};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1764476}.
CC -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC N1-histidyl FAD linkage. {ECO:0000269|PubMed:16154992,
CC ECO:0000269|PubMed:18768475}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AY573966; AAS79317.1; -; mRNA.
DR PDB; 1ZR6; X-ray; 1.55 A; A=26-499.
DR PDB; 2AXR; X-ray; 1.98 A; A=26-499.
DR PDB; 3HSU; X-ray; 1.69 A; A=26-499.
DR PDBsum; 1ZR6; -.
DR PDBsum; 2AXR; -.
DR PDBsum; 3HSU; -.
DR AlphaFoldDB; Q6PW77; -.
DR SMR; Q6PW77; -.
DR CAZy; AA7; Auxiliary Activities 7.
DR iPTMnet; Q6PW77; -.
DR BRENDA; 1.1.99.B3; 10953.
DR EvolutionaryTrace; Q6PW77; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.43.10; -; 1.
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; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW Glycoprotein; Metal-binding; Nucleotide-binding; Oxidoreductase; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:1764476"
FT CHAIN 26..499
FT /note="Glucooligosaccharide oxidase"
FT /id="PRO_5004278602"
FT DOMAIN 58..230
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 454
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:16154992"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16154992,
FT ECO:0007744|PDB:2AXR"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16154992,
FT ECO:0007744|PDB:2AXR"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16154992,
FT ECO:0007744|PDB:2AXR"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16154992,
FT ECO:0007744|PDB:2AXR"
FT BINDING 409
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16154992,
FT ECO:0007744|PDB:2AXR"
FT BINDING 454
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16154992,
FT ECO:0007744|PDB:2AXR"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16154992,
FT ECO:0007744|PDB:1ZR6, ECO:0007744|PDB:2AXR,
FT ECO:0007744|PDB:3HSU"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16154992,
FT ECO:0007744|PDB:1ZR6, ECO:0007744|PDB:2AXR,
FT ECO:0007744|PDB:3HSU"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 31..80
FT /evidence="ECO:0007744|PDB:1ZR6, ECO:0007744|PDB:2AXR,
FT ECO:0007744|PDB:3HSU"
FT CROSSLNK 95..155
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000269|PubMed:16154992,
FT ECO:0000269|PubMed:18768475"
FT MUTAGEN 95
FT /note="H->A,S,C,Y: Does not abolish the covalent FAD
FT linkage and has little effect on the Km, but significantly
FT reduced kcat values 50- to 600-fold. Abolishes FAD binding;
FT when associated with A-155."
FT /evidence="ECO:0000269|PubMed:16332885,
FT ECO:0000269|PubMed:18768475"
FT MUTAGEN 155
FT /note="C->A: Abolishes FAD binding; when associated with A-
FT 95."
FT /evidence="ECO:0000269|PubMed:18768475"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1ZR6"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 245..261
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 306..314
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 341..350
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 353..365
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 373..381
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:1ZR6"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 405..414
FT /evidence="ECO:0007829|PDB:1ZR6"
FT TURN 415..419
FT /evidence="ECO:0007829|PDB:1ZR6"
FT TURN 422..426
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 430..440
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 452..454
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 461..469
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:1ZR6"
FT HELIX 473..483
FT /evidence="ECO:0007829|PDB:1ZR6"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:2AXR"
SQ SEQUENCE 499 AA; 55237 MW; BCB56CF1F4E922CE CRC64;
MVRIQELTAA LSLASVVQAS WIQKRNSINA CLAAADVEFH EEDSEGWDMD GTAFNLRVDY
DPAAIAIPRS TEDIAAAVQC GLDAGVQISA KGGGHSYGSY GFGGEDGHLM LELDRMYRVS
VDDNNVATIQ GGARLGYTAL ELLDQGNRAL SHGTCPAVGV GGHVLGGGYG FATHTHGLTL
DWLIGATVVL ADASIVHVSE TENADLFWAL RGGGGGFAIV SEFEFNTFEA PEIITTYQVT
TTWNRKQHVA GLKALQDWAQ NTMPRELSMR LEINANALNW EGNFFGNAKD LKKILQPIMK
KAGGKSTISK LVETDWYGQI NTYLYGADLN ITYNYDVHEY FYANSLTAPR LSDEAIQAFV
DYKFDNSSVR PGRGWWIQWD FHGGKNSALA AVSNDETAYA HRDQLWLWQF YDSIYDYENN
TSPYPESGFE FMQGFVATIE DTLPEDRKGK YFNYADTTLT KEEAQKLYWR GNLEKLQAIK
AKYDPEDVFG NVVSVEPIA
