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Database: UniProt
Entry: W9S956_9ROSA
LinkDB: W9S956_9ROSA
Original site: W9S956_9ROSA 
ID   W9S956_9ROSA            Unreviewed;       580 AA.
AC   W9S956;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Protein HOTHEAD {ECO:0000313|EMBL:EXC17781.1};
GN   ORFNames=L484_023132 {ECO:0000313|EMBL:EXC17781.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC17781.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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; KE345823; EXC17781.1; -; Genomic_DNA.
DR   RefSeq; XP_010108049.1; XM_010109747.1.
DR   AlphaFoldDB; W9S956; -.
DR   STRING; 981085.W9S956; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   Proteomes; UP000030645; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046593; F:mandelonitrile lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.30.410.40; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; PTHR45968:SF3; OS04G0573100 PROTEIN; 1.
DR   PANTHER; PTHR45968; OSJNBA0019K04.7 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; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000137-3};
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          282..296
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         124
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         237
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         514..515
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         543
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         554..555
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        451..506
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   580 AA;  63012 MW;  5BB7A38824D7604A CRC64;
     MEDNIGRWRL FAAALTGSIF FFFSSLSAAQ KGPNYTFMHN ATTAPDISYY DYIIVGGGTA
     GCPLAATLSQ NYSVLLLERG GSPYGNPNIT NLSAFGAALS DTSPTSPSQR FISEDGVINS
     RARVLGGGSC LNAGFYTRAG TDYVREVGWD GRLVNESYHW VERVVAFEPP MGQWQSAVRD
     GLLEVGVQPY NGFTYDHIVG TKVGGTIFDR DGHRHTAADL LQYANPTGLT VLLHATVHKV
     LFRTKGRQRP SAHGVAFRDA SGIRHRAYLT NGPRSEIIIS SGALGSPQLL MLSGVGPAQH
     LQAHNITVVL DQPMVGQGMS DNPMNSIFIP SPIPVEVSLI EVVGITGFGS YIEAAGGENF
     AGGNPRDYGM FSPKIGQLAT VPPKERTPEA LARAVQLMDS LEDAAFRGGF LLEKIMGPIS
     TGHLELRTRN PNDNPAVTFN YFKETLDLQR CVQGISTIER IIESKSFSRF RYDYMSVPTL
     LNMTASSPIN LLPKHANSST SLEQFCKDTV MTIWHYHGGC QVGRVVDTDY KVLGVDALRV
     IDGSTFSYSP GTNPQATVMM LGRYMGVRIL GERLDAEESK
//
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