ID A0A1R3HKC0_COCAP Unreviewed; 592 AA.
AC A0A1R3HKC0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=CCACVL1_18671 {ECO:0000313|EMBL:OMO70751.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO70751.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO70751.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO70751.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:OMO70751.1}.
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DR EMBL; AWWV01011766; OMO70751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3HKC0; -.
DR STRING; 210143.A0A1R3HKC0; -.
DR EnsemblPlants; OMO70751; OMO70751; CCACVL1_18671.
DR Gramene; OMO70751; OMO70751; CCACVL1_18671.
DR OMA; NYPWIHI; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000188268; 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 GO; GO:0007267; P:cell-cell signaling; IEA:EnsemblPlants.
DR GO; GO:0009553; P:embryo sac development; IEA:EnsemblPlants.
DR GO; GO:0010430; P:fatty acid omega-oxidation; IEA:EnsemblPlants.
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:UP000188268};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..592
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010160087"
FT DOMAIN 292..306
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 89..90
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 248
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 555
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 462..518
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 592 AA; 64761 MW; 27099FF301D75C51 CRC64;
MAAFVGAVKL FLCLVLCLLT LSSLQAGAKD FYEFRYPFIK RASSFSSSAS FSSSNADEVS
YDYIIVGGGT AGCPLAATLS QNFTVLLLER GGVPFSNANV SFLSNFHIAL ADTSPSSASQ
PFVSTDGVLN ARARVLGGGT CINAGFYTRA NSDFIRRVGW DARLVNESYP WVEKQIVHQP
KLAQWQTAFK DSLLDVGISP YNGFTYDHIY GTKVGGTIFD RFGRRHTAAE LLASANPKTL
SVLVYATVQK VLFDKTGKRP RAMGVIFKDE NGNQHQAFLT NNKRSEVILS CGAIATPQLL
MLSGVGPKAE LNKLNISMVM HNEFVGKGMA DNPMNSVFVP TKQPVEQSLI QTVGITKMGV
YIEASSGFGQ SPDSIRCHHG ISSAEIGQLS TIPPKQRTPE AIQAFLRRKK ELPHEAFNGG
FILEKIARPL STGHLSLVNT NIDDNPSVTF NYFGHPHDLK RCVDGIRTVA KVIQSNPFTN
FTKCDKPTVE KLLNMSVKAN INFIPKHTND TKSLEQFCRD TVITIWHYHG GCHVGKVVNP
DLRVLGINRL RIVDGSTFNE SPGTNPQGTV LMMGRYMGIK ILRRRLGRAA GV
//
