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Database: UniProt
Entry: F9WZZ8_ZYMTI
LinkDB: F9WZZ8_ZYMTI
Original site: F9WZZ8_ZYMTI 
ID   F9WZZ8_ZYMTI            Unreviewed;       578 AA.
AC   F9WZZ8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:EGP92460.1};
GN   ORFNames=MYCGRDRAFT_34982 {ECO:0000313|EMBL:EGP92460.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP92460.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP92460.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CM001196; EGP92460.1; -; Genomic_DNA.
DR   RefSeq; XP_003857484.1; XM_003857436.1.
DR   AlphaFoldDB; F9WZZ8; -.
DR   STRING; 336722.F9WZZ8; -.
DR   EnsemblFungi; Mycgr3T34982; Mycgr3P34982; Mycgr3G34982.
DR   GeneID; 13403055; -.
DR   KEGG; ztr:MYCGRDRAFT_34982; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_6_3_1; -.
DR   InParanoid; F9WZZ8; -.
DR   OMA; PSMMNHE; -.
DR   OrthoDB; 3215324at2759; -.
DR   Proteomes; UP000008062; Chromosome 1.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 2.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..578
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003391041"
FT   DOMAIN          269..283
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         250
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         511..512
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   578 AA;  62966 MW;  F271DBA8CDDF764A CRC64;
     MFTHTAPAIL LGVLSTANLV AANPPGPPYF STFQYQFAPA IDFEPSYDFC IVGGGTAGLV
     LANRLTESGK HNVIVFEGGP TPDTNPTSLT GGANPYLLNG ARSLVDYNFV TQPQRNLNNR
     SLPYHRGRCL GGSSATNGFF YGLGSKAVYD QWELDGNPGW NWANISAAAK RGTMFVGNPN
     NTNDNTYMTW DPENYGTEGP LKVGFQGFVP ASNPAFMNAT SAIGVGVVHD QNGGSPTDSG
     EQEATGLTFV EGAIWHNISC SKEVILSAGA FHSPYLLKQS GIGPRDELEE HEIPVRVENE
     HVGHHMQDHT AFSVIYSIKP EFAHIASTTE KNNDLTLLNE QQRSFYNTSD PHERAKSRWS
     AVSGTNAFQE ICSEDLKEFG AGAVIDAGLV SQAHNEIMYE GGWYPFFSNK YGKPRRNTSY
     VSLTVSNMAA LSQGSVTVGN NMPLGDPVID PNYLNHTADI AMAIQGLKYV RKIGQHPDWQ
     KWVAEEVAPG PGVQTDEEIL EYVKTVMIPN WHAASTCRML PKEKGGVVDS HLRVYGTKRL
     RVCDVSTLGR LPDINLQGSV YAVAEHGARI IREEYGDL
//
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