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Database: UniProt
Entry: A0A2I0AEP7_9ASPA
LinkDB: A0A2I0AEP7_9ASPA
Original site: A0A2I0AEP7_9ASPA 
ID   A0A2I0AEP7_9ASPA        Unreviewed;       648 AA.
AC   A0A2I0AEP7;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Protein HOTHEAD {ECO:0000313|EMBL:PKA53985.1};
DE            EC=1.1.-.- {ECO:0000313|EMBL:PKA53985.1};
GN   Name=HTH {ECO:0000313|EMBL:PKA53985.1};
GN   ORFNames=AXF42_Ash016150 {ECO:0000313|EMBL:PKA53985.1};
OS   Apostasia shenzhenica.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Apostasioideae; Apostasia.
OX   NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA53985.1, ECO:0000313|Proteomes:UP000236161};
RN   [1] {ECO:0000313|EMBL:PKA53985.1, ECO:0000313|Proteomes:UP000236161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC   TISSUE=Stem {ECO:0000313|EMBL:PKA53985.1};
RX   PubMed=28902843; DOI=10.1038/nature23897;
RA   Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA   Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA   Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA   Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA   Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA   Van de Peer Y., Liu Z.J.;
RT   "The Apostasia genome and the evolution of orchids.";
RL   Nature 549:379-383(2017).
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; KZ451987; PKA53985.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0AEP7; -.
DR   STRING; 1088818.A0A2I0AEP7; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000236161; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000313|EMBL:PKA53985.1};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236161};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        36..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          338..352
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         177
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         582..583
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         611
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         622..623
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        519..574
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   648 AA;  71018 MW;  3DCFF6E87A0023D0 CRC64;
     MAVGCRQPPR EFGPPSLGCH RSSSPIYFLS LSPPPSIESL YFFFFFFFFF KEIDQMGIRR
     LQGEWFLLLL LLLLCFVGCC HSEQAPNYTF VKQATEAPAV SYYDYIIVGG GTAGCPLAAT
     LSRTSDVLLL ERGGSPYGNK NISNLAFFAD TLADVSPTSP SQRFVSEDGV FNARARVLGG
     GSCLNAGFYT RAGADYIRGA GWDATLVEES YRWVEKVVAF EPPVRQWQSA VRDGLLEVGI
     TPYNGFTYDH LYGTKVGGTI FDRNGYRHTA ADLLAYADPA RLTVLLRATA ERIVWRGDGK
     GRRGRPAAQG VVFVDSAGRR RQAYLRKGKG SEVIVAAGAM GSPQLLMLSG VGPREGLERL
     GIGVVAERDM VGKGMADNPM NAIFVPSPAP VEVSLIQVVG ITRFGTYIEA ASGQYFGSPS
     NSGGDGDAAR PPAKNFGIFS PQTGQLSTVP PKQRTQEALD RAARAMARLD PAAFQGGFIL
     EKIVGPVSRG HLELRTRDPH DNPSVTFNYF QDPIDLRRCV DGIKTIEKVI QSKAFDRFRY
     PDISIQALAN MTARFPVNLL PRHDNDSRSP EQFCRDTVMT IWHYHGGCQV GRVVDGDYRV
     LGVDALRVID GSTFNFSPGT NPQATVMMLG RYMGVKILEE RLRATEED
//
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