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}.
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 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
//