CHITO_GIBZE
ID CHITO_GIBZE Reviewed; 492 AA.
AC I1S2K2; A0A098E050;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Chitooligosaccharide oxidase {ECO:0000303|PubMed:17900572};
DE EC=1.1.3.- {ECO:0000269|PubMed:17900572};
DE Flags: Precursor;
GN Name=chitO {ECO:0000303|PubMed:17900572}; ORFNames=FGRAMPH1_01T20975;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP MUTAGENESIS OF GLN-268.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17900572; DOI=10.1016/j.febslet.2007.09.019;
RA Heuts D.P.H.M., Janssen D.B., Fraaije M.W.;
RT "Changing the substrate specificity of a chitooligosaccharide oxidase from
RT Fusarium graminearum by model-inspired site-directed mutagenesis.";
RL FEBS Lett. 581:4905-4909(2007).
CC -!- FUNCTION: Catalyzes the selective oxidation of C1 hydroxyl moieties on
CC chitooligosaccharides with concomitant reduction of molecular oxygen to
CC hydrogen peroxide. This results in the formation of the corresponding
CC lactones, which typically undergo spontaneous hydrolysis.
CC Chitooligosaccharides are homo- or heterooligomers of N-
CC acetylglucosamine (GlcNAc) and D-glucosamine which are linked through
CC beta-1,4-glycosidic bonds. For optimal substrate binding at least 2
CC GlcNAc units are needed, and chitooligosaccharide oxidase is most
CC efficient on chitobiose, chitotriose and chitotetraose.
CC {ECO:0000269|PubMed:17900572}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N,N'-diacetylchitobiose + O2 = H2O2 + N,N'-diacetylchitobiono-
CC 1,5-lactone; Xref=Rhea:RHEA:59544, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28681, ChEBI:CHEBI:143145;
CC Evidence={ECO:0000269|PubMed:17900572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N,N',N''-triacetylchitotriose + O2 = H2O2 + N,N',N''-
CC triacetylchitotriono-1,5-lactone; Xref=Rhea:RHEA:59548,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:143141,
CC ChEBI:CHEBI:143144; Evidence={ECO:0000269|PubMed:17900572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N,N',N'',N'''-tetraacetylchitotetraose + O2 = H2O2 +
CC N,N',N'',N'''-tetraacetylchitotetraono-1,5-lactone;
CC Xref=Rhea:RHEA:59552, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:143142, ChEBI:CHEBI:143143;
CC Evidence={ECO:0000269|PubMed:17900572};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17900572};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000269|PubMed:17900572};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.3 mM for GlcNAc {ECO:0000269|PubMed:17900572};
CC KM=0.30 mM for N,N'-diacetylchitobiose {ECO:0000269|PubMed:17900572};
CC KM=0.26 mM for N,N',N''-triacetylchitotriose
CC {ECO:0000269|PubMed:17900572};
CC KM=0.25 mM for N,N',N'',N'''-tetraacetylchitotetraose
CC {ECO:0000269|PubMed:17900572};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6PW77}.
CC -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC N1-histidyl FAD linkage. {ECO:0000250|UniProtKB:Q6PW77}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; HG970334; CEF87481.1; -; Genomic_DNA.
DR RefSeq; XP_011325372.1; XM_011327070.1.
DR PDB; 6Y0R; X-ray; 1.61 A; AAA=1-492.
DR PDBsum; 6Y0R; -.
DR AlphaFoldDB; I1S2K2; -.
DR SMR; I1S2K2; -.
DR STRING; 229533.I1S2K2; -.
DR GeneID; 23557872; -.
DR KEGG; fgr:FGSG_10998; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G20975; -.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_10_1_1; -.
DR InParanoid; I1S2K2; -.
DR Proteomes; UP000070720; Chromosome 3.
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; FAD; Flavoprotein; Oxidoreductase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..492
FT /note="Chitooligosaccharide oxidase"
FT /id="PRO_5010968455"
FT DOMAIN 57..229
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CROSSLNK 94..154
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:Q6PW77"
FT MUTAGEN 268
FT /note="Q->R: Changes substrate affinity from N-acetylated
FT towards non-acetylated oligosaccharides."
FT /evidence="ECO:0000269|PubMed:17900572"
SQ SEQUENCE 492 AA; 52612 MW; A1ECD7A8E1959323 CRC64;
MHFNTLTCVL VGLVAHTSAV PTKREAVNSC LTQAKVPTDA QGSQSWKEDG TAYNLRLPFE
PAAIAVPTTV AQVSAAVECG AKHGVAISAK SGGHSYTSLG FGGEDGHLMI ELDRMYSVKL
AKDGTAKIQP GARLGHVATE LWNQGKRALA HGTCPGVGLG GHALHGGYGM VARKHGLTLD
LMIGATVVLP TGKVVHCSKT ENSDLFWGIR GAGANFGVVV ELEFQTFAAP EKITYFDIGL
NWDQNTAPQG LYDFQEFGKG MPAEITMQMG VSKNGYSVDG AYIGDEASLR KALQPLVQKF
GGVQVTATTV DWMGLVTHFA GAGVNVNPTS ASYDAHDNFY ASSLAAPALT LAEFKSFVNF
VSTTGKSSSH SWWLQMDITG GTYSAVSKPK PSDTAYVHRD TLLLFQFYDS VAATAQYPSD
GFNLIKGLRQ SISSSLKAGT WGMYANYPDS QIKNDRATEM YWGSNVAKLE AVKAKYDPKN
LFRNPQSIKP KA
