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Database: UniProt
Entry: A0A1S4BQC6_TOBAC
LinkDB: A0A1S4BQC6_TOBAC
Original site: A0A1S4BQC6_TOBAC 
ID   A0A1S4BQC6_TOBAC        Unreviewed;       596 AA.
AC   A0A1S4BQC6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Protein HOTHEAD-like isoform X2 {ECO:0000313|RefSeq:XP_016491071.1};
GN   Name=LOC107810756 {ECO:0000313|RefSeq:XP_016491071.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016491071.1};
RN   [1] {ECO:0000313|Proteomes:UP000084051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [2] {ECO:0000313|RefSeq:XP_016491071.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_016491071.1; XM_016635585.1.
DR   AlphaFoldDB; A0A1S4BQC6; -.
DR   GeneID; 107810756; -.
DR   OMA; TYSPFFW; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000084051; Unplaced.
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; OSJNBA0019K04.7 PROTEIN; 1.
DR   PANTHER; PTHR45968:SF5; PROTEIN HOTHEAD; 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:UP000084051};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..596
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010186490"
FT   DOMAIN          296..310
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         93..94
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         139
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         252
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         530..531
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         559
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         570..571
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        466..522
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   596 AA;  65218 MW;  8F1B05FADA71AD44 CRC64;
     MAVVGGAAAL PLIFKLLLSL LLCFNSSPSL TQAGKWVPWE DRYPFIREAS SFSSSSNNAN
     NNKAYDYIIV GGGTAGCPLA ATLSQKFSVL LLERGGVPFA NANVSFMQNF HIALADTSPS
     SASQYFVSTD GVFNSRARVL GGGTCINAGF YTRAGPSYIK KAGWDSKLVN ESYPWIEKQI
     VHRPNLAPWQ RAVRDSLLEI GISPFNGFTY DHIYGTKVGG TIFDRFGRRH TAAELLASAN
     PKKLDVLVHA TVQKIDFDTS GKKPRAVGVI FKDENGNQHK AFLSKRKGSE IIVSSGAIGS
     PHILMLSGIG PKAELEKLNI PVVLDNKFVG QGMSDNPLNT IFVPTNRHVE QSLIQTVGIT
     KAGVYIEASS GFGQSGDSIR CNHGVASAEI GQLSTIPPKQ RTFEAIEAYR RSKKNIPHEL
     FRGGFILEKI ATPLSRGNIS LVTTNADDNP SITFNYFSHP RDLKRCVDGI RIVEKIAKSK
     HFTNYTQCDK ETLDKLLNMS VQANVNLIPK HTNNTQSLEQ FCKDTVITIW HYHGGCHVGK
     VIAPDYRVLG VHRLRVIDGS TFEESPGTNP QATVMMMGRY MGVKILRERL GRTAGL
//
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