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Database: UniProt
Entry: V4LLJ3_EUTSA
LinkDB: V4LLJ3_EUTSA
Original site: V4LLJ3_EUTSA 
ID   V4LLJ3_EUTSA            Unreviewed;       556 AA.
AC   V4LLJ3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=EUTSA_v10015625mg {ECO:0000313|EMBL:ESQ43337.1};
OS   Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX   NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ43337.1, ECO:0000313|Proteomes:UP000030689};
RN   [1] {ECO:0000313|EMBL:ESQ43337.1, ECO:0000313|Proteomes:UP000030689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA   Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA   Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA   Mitchell-Olds T., Schumaker K.S., Wang X.;
RT   "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL   Front. Plant Sci. 4:46-46(2013).
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}.
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DR   EMBL; KI517464; ESQ43337.1; -; Genomic_DNA.
DR   RefSeq; XP_006401884.1; XM_006401821.1.
DR   AlphaFoldDB; V4LLJ3; -.
DR   STRING; 72664.V4LLJ3; -.
DR   EnsemblPlants; ESQ43337; ESQ43337; EUTSA_v10015625mg.
DR   GeneID; 18016411; -.
DR   Gramene; ESQ43337; ESQ43337; EUTSA_v10015625mg.
DR   KEGG; eus:EUTSA_v10015625mg; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   OMA; NAMMYHH; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000030689; 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:SF38; GLUCOSE-METHANOL-CHOLINE (GMC) OXIDOREDUCTASE FAMILY 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; 2.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000030689};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          244..258
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          532..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         22..23
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         41..42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         87
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         200
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         472..473
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         501
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         512..513
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        409..464
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   556 AA;  61324 MW;  7B3709EE40E54C33 CRC64;
     MKDATSAPTY ARFDYIVIGG GTSGCSLAAT LSQNANVLVL ERGGSPYDNP TATDMENFAN
     TLLNVTPNSW SQTFISEDGV YNTRARVLGG DSVLNAGFYS RAENSYVEEA EWEKEEVEAA
     YEWVERKLVF EPQVMGWQSA LRDGLLEAGV LPYNGFTLDH IVGTKIGGTI FDPAGHRHSA
     ADLLEYANPE KLVVYMHALV HKILFTKGDQ IPKAYGVVYQ DTDGVFHKAE LARNTMNEVI
     LCAGALGSPQ LLMLSGVGPK AHLEAHGIHP VVLDHPMVGQ GMGDNPMNSV VVPSPQLVDL
     SLVEVVGITK FHSFIEGFSG LSLSYNLTRR FFDGTLNLLH ESSLSTQSIT NFFKSIDLRL
     NVMENHGVIM NKVDGPVSRG HLELRNMNPD DNPSVTFNYY KEPEDLKVCV KGLKTVIKVI
     NSNAFSKYKY PNATGRELLN LMLSLPINLR PRHKTAMFNL TQFCIDTVVT IWHYHGGCQI
     GRVVDNNYKV FGIDALRVID GSTFLKSPGT NPQATVMMLG RYMGQKILRE RNASGEKNQD
     DSIIKDGTNM WSSSSK
//
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