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Database: UniProt
Entry: A0A445HW68_GLYSO
LinkDB: A0A445HW68_GLYSO
Original site: A0A445HW68_GLYSO 
ID   A0A445HW68_GLYSO        Unreviewed;       564 AA.
AC   A0A445HW68;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Protein HOTHEAD isoform B {ECO:0000313|EMBL:RZB78006.1};
GN   ORFNames=D0Y65_028788 {ECO:0000313|EMBL:RZB78006.1};
OS   Glycine soja (Wild soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3848 {ECO:0000313|EMBL:RZB78006.1, ECO:0000313|Proteomes:UP000289340};
RN   [1] {ECO:0000313|EMBL:RZB78006.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB78006.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-2018) 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}.
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:RZB78006.1}.
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DR   EMBL; QZWG01000011; RZB78006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445HW68; -.
DR   Proteomes; UP000289340; Chromosome 11.
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: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:UP000289340};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..564
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019337917"
FT   DOMAIN          283..297
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         515..516
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         544
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         555..556
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        452..507
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   564 AA;  61630 MW;  5037C1C4BCC4529C CRC64;
     MGIWWWRLIL VSLAGILFSP KHGASQRVTG MKYTFMKNAS SAPSVSYYEY EYIVIGGGTA
     GCPLAATLSE KHKVLVLERG PSPYGNPNIT NLDAFGAALS DTSPNSPSQR FISQDGVINS
     RARVLGGGSC LNAGFYTRAS PYYVREAGWD GKLVKKSYEW VERVVAFEPI VRQWQSAVRG
     GLLEVGVLPY NGFTFDHIRG TKVGGTIFDQ HGHRHTAADL LEYANPTQLT VLLQATVSKI
     LFTNKGSRSR PVASGVIFMD ALGREHRVYL KQGPKSEIIV SAGALGSPQL LMLSGIGAER
     ELRKHNIDVV LNQPLVGQGM SDNPMNAIFV PSPVPVEVSL IEVVGITNVG SYIEAASGQM
     FTSRSPRDYG MFSPKIGQFS KLPPKQRSPE AVAKAIEKMG MLEPAAFRGG FILEKIMGPI
     STGELQLETS DPNDNPSVSF NYFKDPRDLK RCVQGIRTIE KVIESKAFSR FRYHNMSASV
     LLNMTANSPV NLLPKHSNTA TSLEQFCRDT VMTIWHYHGG CQVGRVVDAR YKVIGVDALR
     VIDGSTFNCS PGTNPQATVM MLGR
//
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