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Database: UniProt
Entry: A0A1U8AA87_NELNU
LinkDB: A0A1U8AA87_NELNU
Original site: A0A1U8AA87_NELNU 
ID   A0A1U8AA87_NELNU        Unreviewed;       588 AA.
AC   A0A1U8AA87;
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-like {ECO:0000313|RefSeq:XP_010262118.1};
GN   Name=LOC104600715 {ECO:0000313|RefSeq:XP_010262118.1};
OS   Nelumbo nucifera (Sacred lotus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX   NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010262118.1};
RN   [1] {ECO:0000313|RefSeq:XP_010262118.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_010262118.1; XM_010263816.2.
DR   AlphaFoldDB; A0A1U8AA87; -.
DR   STRING; 4432.A0A1U8AA87; -.
DR   GeneID; 104600715; -.
DR   KEGG; nnu:104600715; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   InParanoid; A0A1U8AA87; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000189703; 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:UP000189703};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..588
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010534030"
FT   DOMAIN          288..302
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         131
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         244
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         522..523
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         551
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         562..563
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        458..514
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   588 AA;  64208 MW;  2B773D32BA365FAF CRC64;
     MASLGIVKLF LNIFFCLNLL ASSAQGKEDY SKYRYPFIKA ASSFTSSRTW TGNDSPYDYI
     IVGGGTAGCP LAATLSEKFR VLLLERGDAP FANLNVSYLQ NFHISLADTS PTSASQAFIS
     TDGVINARAR VLGGGTCINA GFYTRATPGF IKKAGWDSEI VKESYPWIEK QIVRWPQVAP
     WQEALRNGLL EVGVSPFNGF TYDHIYGTKI GGTTFDKSGR RYTAAHLLAS ANPENLRVLV
     HATVEKILFD KTGRQPRAVG VVFKDEYGNR HQAFVSKRME SEVILSSGAI GSPQLLLLSG
     IGPATDLKRM NIPVVLHNEF VGKGMSDNPM NSIFVPTKKP VKQSLIETVG ITKMGVFIEG
     SSGFGQSSDS IQCNHGIMSA EIGQLSTVPP KQRTPEAIKA YIESKQSLPH EAFMGGFVLE
     KIVGPLSTGE LSLISTDVDD NPSVTFNYFS HPYDLKRCVY GIRMIEKVVQ TKHFADLINS
     DMPAVEMLLN MSIKANVNLI PKQTNDTKSL EQFCKDTVTT IWHYHGGCHV GKVVDAKYKV
     LGVDGLRVVD GSIFNTSPGT NPQATVMMMG RYMGVKILRE PLGRAAGV
//
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