ID A0A3B5XZ80_WHEAT Unreviewed; 588 AA.
AC A0A3B5XZ80;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS1A02G187500.1};
RN [1] {ECO:0000313|EnsemblPlants:TraesCS1A02G187500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS1A02G187500.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS1A02G187500.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) 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}.
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 AlphaFoldDB; A0A3B5XZ80; -.
DR SMR; A0A3B5XZ80; -.
DR STRING; 4565.A0A3B5XZ80; -.
DR PaxDb; 4565-Traes_1AL_D8E27B4FC-1; -.
DR EnsemblPlants; TraesCS1A02G187500.1; TraesCS1A02G187500.1; TraesCS1A02G187500.
DR Gramene; TraesCS1A02G187500.1; TraesCS1A02G187500.1; TraesCS1A02G187500.
DR Gramene; TraesCS1A03G0503800.1; TraesCS1A03G0503800.1.CDS; TraesCS1A03G0503800.
DR Gramene; TraesPAR_scaffold_003613_01G000300.1; TraesPAR_scaffold_003613_01G000300.1; TraesPAR_scaffold_003613_01G000300.
DR OMA; KGAFCNP; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000019116; Chromosome 1A.
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:SF6; PROTEIN, PUTATIVE, EXPRESSED-RELATED; 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:UP000019116};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..588
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017434484"
FT DOMAIN 288..302
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 66..67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 242
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 526..527
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 566..567
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 463..518
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 588 AA; 63802 MW; 36B08FB75A9695E2 CRC64;
MPSSPAQMAL GRARSPALVL AAAVLGALCV VALSEDEQLE NLRFVQHAQD APLVSHYNYI
VVGGGTSGCP LAATLSEHSR VLLLERGGLP YRNMSNQEHF TDALADTSLA SPAQRFVSTD
GVVNARARVL GGGSCLNAGF YTRASNEYVR TAGWDAGLVN SSYRWVERAL VFRPDVPPWQ
AALRDALLEA GVTPDNGFTF DHVTGTKIGG TIFDNNGQRH TAADFLRHAR PRGLTVVLYA
TVSRVLFRSQ EGVPYPVAYG VVFADPLGVQ HRVYLRDGGK NEVILSAGTL GSPQLLMLSG
VGPQVHLEAH GIQVLVDQPM VGQGVADNPM NSVFIPSPVP VGLSLVQVVG ITKSGSFIEG
VSGSEFGIPV SDGARRLASF GLFSPQTGQL GTLPPGQRTP EALQRAAEAM RRLDRRAFRG
GFILEKILGP VSTGHIELRS TDPRANPAVT FNYFQEAEDL ERCVRGIQTI ERVIQSRAFS
NFTYANTTVE SIFTDSANFP VNLLPRHVND SRSPEQYCRE TVMTIWHYHG GCHVGAVVDD
NYRVFGVRGL RVIDSSTFRY SPGTNPQATV MMLGRYMGIK IQAERWRK
//
