MNCO_MICNN
ID MNCO_MICNN Reviewed; 495 AA.
AC I1SB12;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 2.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Carbohydrate oxidase {ECO:0000303|PubMed:11179980};
DE EC=1.1.3.-;
DE EC=1.1.3.5 {ECO:0000269|PubMed:11179980};
DE AltName: Full=Lactose oxidase {ECO:0000303|PubMed:17154316};
DE Short=LaO;
DE Flags: Precursor;
GN Name=MnCO {ECO:0000303|PubMed:11179980};
OS Microdochium nivale (Pink snow mold) (Lanosa nivalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=5520;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-46; 217-292;
RP 325-344; 358-369; 404-435 AND 442-462, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=NN008551;
RX PubMed=11179980; DOI=10.1046/j.1432-1327.2001.01982.x;
RA Xu F., Golightly E.J., Fuglsang C.C., Schneider P., Duke K.R., Lam L.,
RA Christensen S., Brown K.M., Joergensen C.T., Brown S.H.;
RT "A novel carbohydrate:acceptor oxidoreductase from Microdochium nivale.";
RL Eur. J. Biochem. 268:1136-1142(2001).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX DOI=10.1016/S1381-1177(00)00233-2;
RA Kulys J., Tetianec L., Schneider P.;
RT "Specificity and kinetic parameters of recombinant Microdochium nivale
RT carbohydrate oxidase.";
RL J. Mol. Catal., B Enzym. 13:95-101(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RA Tetianec L., Kulys J.;
RT "The specificity of recombinant Microdochium nivale carbohydrate oxidase.";
RL Biologija 2:38-41(2003).
RN [4]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=17154316; DOI=10.1002/bit.21273;
RA Nordkvist M., Nielsen P.M., Villadsen J.;
RT "Oxidation of lactose to lactobionic acid by a Microdochium nivale
RT carbohydrate oxidase: kinetics and operational stability.";
RL Biotechnol. Bioeng. 97:694-707(2007).
RN [5]
RP CRYSTALLIZATION.
RX PubMed=19478452; DOI=10.1107/s1744309109017643;
RA Duskova J., Dohnalek J., Skalova T., Oestergaard L.H., Fuglsang C.C.,
RA Kolenko P., Stepankova A., Hasek J.;
RT "Crystallization of carbohydrate oxidase from Microdochium nivale.";
RL Acta Crystallogr. F 65:638-640(2009).
RN [6] {ECO:0007744|PDB:3RJ8, ECO:0007744|PDB:3RJA}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 23-495 IN COMPLEX WITH FAD, AND
RP GLYCOSYLATION AT ASN-244.
RA Duskova J., Skalova T., Kolenko P., Stepankova A., Hasek J., Koval T.,
RA Ostergaard L.H., Fuglsang C.C., Dohnalek J.;
RT "Crystal structure and kinetic studies of carbohydrate oxidase from
RT Microdochium nivale.";
RL Submitted (APR-2011) to the PDB data bank.
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. Carbohydrate oxidase is able to oxidize a variety of
CC substrates including D-glucose, D-galactose, D-xylose, D-maltose, D-
CC cellobiose, and lactose. In addition, among various oligosaccharides,
CC the enzyme preferred tetrameric dextrins, indicating a favorable
CC interaction of four linked glucose units with the substrate binding
CC pocket. {ECO:0000269|PubMed:11179980, ECO:0000269|Ref.2,
CC ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:11428, ChEBI:CHEBI:15379, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:16217, ChEBI:CHEBI:16240; EC=1.1.3.5;
CC Evidence={ECO:0000269|PubMed:11179980};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose + O2 = D-galactono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59312, ChEBI:CHEBI:4139, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15945, ChEBI:CHEBI:16240; EC=1.1.3.5;
CC Evidence={ECO:0000269|PubMed:11179980};
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; EC=1.1.3.5;
CC Evidence={ECO:0000269|PubMed:11179980, ECO:0000269|Ref.3};
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; EC=1.1.3.5;
CC Evidence={ECO:0000269|PubMed:11179980};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-maltose + O2 = D-maltobiono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59344, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17306, ChEBI:CHEBI:143029; EC=1.1.3.5;
CC Evidence={ECO:0000269|PubMed:11179980, ECO:0000269|Ref.3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylose + O2 = D-xylono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:59324, ChEBI:CHEBI:15379, ChEBI:CHEBI:15867,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:53455;
CC Evidence={ECO:0000269|PubMed:11179980};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17154316};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000269|Ref.6};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.97 mM for oxygen {ECO:0000269|PubMed:17154316};
CC KM=19 mM for cellobiose (at pH 6 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:11179980};
CC KM=59 mM for cellobiose (at pH 6 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:11179980};
CC KM=51 uM for cellobiose (at pH 7.2 and 25 degrees Celsius)
CC {ECO:0000269|Ref.3};
CC KM=59 uM for cellotriose (at pH 7.2 and 25 degrees Celsius)
CC {ECO:0000269|Ref.3};
CC KM=66 uM for cellotetraose (at pH 7.2 and 25 degrees Celsius)
CC {ECO:0000269|Ref.3};
CC KM=42 mM for glucose (at pH 6 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:11179980};
CC KM=11 mM for maltose (at pH 6 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:11179980};
CC KM=12 mM for maltose (at pH 7.2 and 25 degrees Celsius)
CC {ECO:0000269|Ref.3};
CC pH dependence:
CC Optimum pH is 5-7. {ECO:0000269|PubMed:11179980};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:11179980};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11179980}.
CC -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC N1-histidyl FAD linkage. {ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR PDB; 3RJ8; X-ray; 2.40 A; A=23-495.
DR PDB; 3RJA; X-ray; 2.10 A; A=23-495.
DR PDBsum; 3RJ8; -.
DR PDBsum; 3RJA; -.
DR AlphaFoldDB; I1SB12; -.
DR SMR; I1SB12; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046562; F:glucose oxidase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; 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; Direct protein sequencing; FAD; Flavoprotein; Glycoprotein;
KW Metal-binding; Nucleotide-binding; Oxidoreductase; Secreted; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:11179980"
FT CHAIN 23..495
FT /note="Carbohydrate oxidase"
FT /id="PRO_0000446664"
FT DOMAIN 55..229
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:3RJ8, ECO:0007744|PDB:3RJA"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CROSSLNK 92..154
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000269|Ref.6"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:3RJA"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 245..261
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 267..277
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 339..349
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 372..381
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:3RJA"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:3RJA"
FT STRAND 405..414
FT /evidence="ECO:0007829|PDB:3RJA"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 425..436
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 457..465
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:3RJA"
FT HELIX 469..479
FT /evidence="ECO:0007829|PDB:3RJA"
SQ SEQUENCE 495 AA; 54679 MW; DBA2FE3B59649BF5 CRC64;
MRSAFILALG LITASADALV TRGAIEACLS AAGVPIDIPG TADYERDVEP FNIRLPYIPT
AIAQTQTTAH IQSAVQCAKK LNLKVSAKSG GHSYASFGFG GENGHLMVQL DRMIDVISYN
DKTGIAHVEP GARLGHLATV LNDKYGRAIS HGTCPGVGIS GHFAHGGFGF SSHMHGLAVD
SVVGVTVVLA DGRIVEASAT ENADLFWGIK GAGSNFGIVA VWKLATFPAP KVLTRFGVTL
NWKNKTSALK GIEAVEDYAR WVAPREVNFR IGDYGAGNPG IEGLYYGTPE QWRAAFQPLL
DTLPAGYVVN PTTSLNWIES VLSYSNFDHV DFITPQPVEN FYAKSLTLKS IKGDAVKNFV
DYYFDVSNKV KDRFWFYQLD VHGGKNSQVT KVTNAETAYP HRDKLWLIQF YDRYDNNQTY
PETSFKFLDG WVNSVTKALP KSDWGMYINY ADPRMDRDYA TKVYYGENLA RLQKLKAKFD
PTDRFYYPQA VRPVK
