ID A0A1U8FUQ4_CAPAN Unreviewed; 599 AA.
AC A0A1U8FUQ4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Protein HOTHEAD {ECO:0000313|EMBL:PHT62174.1};
GN ORFNames=T459_33987 {ECO:0000313|EMBL:PHT62174.1};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072 {ECO:0000313|EMBL:PHT62174.1, ECO:0000313|Proteomes:UP000222542};
RN [1] {ECO:0000313|EMBL:PHT62174.1, ECO:0000313|Proteomes:UP000222542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CM334 {ECO:0000313|Proteomes:UP000222542};
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
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, ECO:0000256|RuleBase:RU003968}.
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:PHT62174.1}.
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DR EMBL; AYRZ02000092; PHT62174.1; -; Genomic_DNA.
DR RefSeq; XP_016562570.1; XM_016707084.1.
DR AlphaFoldDB; A0A1U8FUQ4; -.
DR STRING; 4072.A0A1U8FUQ4; -.
DR EnsemblPlants; PHT62174; PHT62174; T459_33987.
DR GeneID; 107861734; -.
DR Gramene; PHT62174; PHT62174; T459_33987.
DR KEGG; cann:107861734; -.
DR OMA; ECARGKV; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000222542; Unassembled WGS sequence.
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; PS00623; GMC_OXRED_1; 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, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000222542};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..599
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030035557"
FT DOMAIN 140..163
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 299..313
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 96..97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 255
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 533..534
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 562
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 573..574
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 469..525
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 599 AA; 65541 MW; 71B9F47172A2995F CRC64;
MAVVGRLPVI FINQLLLSLL LCLHFTTLIQ GAGKWEDKYP FIREASTFSS SDGTNNESNG
NNNKKGGYDY IIVGGGTAGC PLANTLSQKF RVLLVERGGV PFANANVSFM QNFHISLADT
SSTSASQYFV STDGVFNSRA RILGGGTCIN AGFYTRAGPS YIQKVGWDSK LVNESYPWIE
RQIVHRPNLA PWQEAVRESL LEIGISPFNG FTYDHIYGTK VGGTIFDRFG RRHTAAELLA
TANPKNLDVL VHATVQKIDF DTSGKKPRAV GVIFKDENGK QHKAVLSKRK GSEIIVSCGA
IGSPHILMLS GIGPKAELEK LNIPVVLDNK FVGQGMSDNP LNTIFVPTNR PVEQSLIQTV
GITKVGVYVE ASSGFGQSGD SITCNHGVAS AEIGQLSTIP PKQRTLEAIE AFRRSKKNIP
HEAFRGGFIL EKIASPLSRG NISLVNTNPD DNPSITFNYF SHPRDLKRCV DGIRIVEKIA
KSKHFTNYTQ CDKETLDKLL NMSIQANVNL IPKHTHNTES LEQFCKDTVI TIWHYHGGCH
VGKVIAPDHR VLGVNRLRVI DGSTFKESPG TNPQATVMMM GRYMGVKILR ERLGSAAGL
//
