GenomeNet

Database: UniProt
Entry: M1W4Z3_CLAP2
LinkDB: M1W4Z3_CLAP2
Original site: M1W4Z3_CLAP2 
ID   M1W4Z3_CLAP2            Unreviewed;       631 AA.
AC   M1W4Z3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Related to alcohol oxidase {ECO:0000313|EMBL:CCE29565.1};
GN   ORFNames=CPUR_03412 {ECO:0000313|EMBL:CCE29565.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE29565.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE29565.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE29565.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCE29565.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CAGA01000015; CCE29565.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1W4Z3; -.
DR   STRING; 1111077.M1W4Z3; -.
DR   VEuPathDB; FungiDB:CPUR_03412; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_5_1_1; -.
DR   OrthoDB; 2392848at2759; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
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; 1.
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:SF78; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016801}.
FT   DOMAIN          91..114
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          283..297
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         93
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         234
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         560..561
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   631 AA;  68632 MW;  903336400D628D4F CRC64;
     MDTMGITPAE YDIIIAGGGT VACVVAGRLA EADPTLSILI IEQGQNNLND PAVTTPALFW
     SNLGPESKYA SFYKANKEDS INGREAVVPT GRVLGGGSSI NFMMYARAQA CDFDSWNTEG
     WDSKSLIALA KKLETFHLHG PEYDKSIHGY SGPIGVSYGT YEPLAHHDIT AAAVAVGEKL
     VVDMQNFTTA TGIFRWLRYV SPDGKRQDTA HRYIHPLMTS GKYPNIHLLL NTTVSRVLFQ
     DTRATGVECQ PSIASNATST AGSATTNPST TLTARKLVVV SAGALGSPQL LERSGIGNKE
     ILAPLDIPLV AHLPGVGENY QDHNMVKSSY KVDLPPSETL DAIIGGRLDY AAALLEEHPT
     KTHPILGWNG VDFGARLRPT EPEVAQLGPD FQQLWDRDFK YQTDRPLMLL GAMSTGLGAP
     EEPADAEGRR KHFQYITMIP YTAYPYSRGN IHIVSKDPSC PPCFNTGFLS HSADLKAQLW
     AYKKQREIMR RTNIFHAEVP GCHPKFPKGS KAALMDHHPL GAMSLYASSE DRGNLPALEY
     DADDDAAIEE YIRDRLDTTW HSLGTCKMAP RERGGVVDKD LNVHGVTNLK IADLSICPEN
     VAANTYNTAL IVGEKAAILI GRDLGLTISE S
//
DBGET integrated database retrieval system