ID   A0A1D6I361_MAIZE        Unreviewed;       626 AA.
AC   A0A1D6I361;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Protein HOTHEAD {ECO:0000313|EMBL:ONM54593.1};
GN   ORFNames=ZEAMMB73_Zm00001d020238 {ECO:0000313|EMBL:ONM54593.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM54593.1};
RN   [1] {ECO:0000313|EMBL:ONM54593.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM54593.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CM007650; ONM54593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6I361; -.
DR   ExpressionAtlas; A0A1D6I361; baseline and differential.
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; 3.30.410.40; -; 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:SF1; OS09G0363900 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   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          315..329
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         85..86
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         131
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         269
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"
FT   BINDING         589
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         600..601
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        495..552
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   626 AA;  68619 MW;  080E18F8B39EEE3F CRC64;
     MALSGRALLL FKLLLLLLAC LLFLLELSRG KEEAFSLRNL PPFHKASSYP AGCPTTYDYI
     IVGGGTAGCP LAATLSHRYR VLLLERGGSP YGDRNVSYMQ NFHIGLMNMA PDSPSQAFIS
     TDGVINARAR VLGGGTCINA GFYSRASPRY AMHWMHDVFC TILLVFISCS CTYSFIQEAG
     WDEDLVNKSY PWVEDKIVQW PKIAPWQAAL RDGLLQAGVA PFNGYTYDHV SGTKVGGTIF
     DETGYRHTAA DLLAAGDASN LKVLLHASVH KIVFGSRQGR LKARAIGVEF TDEDGRHHQA
     FLNSNRDSEV IVSAGAIGTP QLLLLSGIGP KNDLKNHNIP VVLHNRYVGK GMADNPMNSI
     FIPTRSPPRQ SLIETVGITE EGVFIEASSG FGQSSESVHC HHGIMSAEPN MLHSCEIQIG
     QLSTIPPKQR TLEAAQKYAH NKLNLPKEVF HGGFILEKID GPMSTGHLVL TDTDVRNNPA
     VTFNYFSHPQ DLNRCIYGIK TIERILKTNR FSELSADGAG LSMERVLNMS VQANVNLIPK
     HTNDTESLEQ FCKDTVITIW HYHGGCHVGK VVDQHYRVLG VSGLRVVDGS IFSKSPGTNP
     QATVMMMGRY MGVKILRERL GRAAGV
//