ID A0A0S3SZT6_PHAAN Unreviewed; 589 AA.
AC A0A0S3SZT6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN Name=Vigan.09G205000 {ECO:0000313|EMBL:BAT98398.1};
GN ORFNames=VIGAN_09205000 {ECO:0000313|EMBL:BAT98398.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT98398.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT98398.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015042; BAT98398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3SZT6; -.
DR Proteomes; UP000291084; Chromosome 9.
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:UP000291084};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..589
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006618815"
FT DOMAIN 289..303
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 86..87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 245
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 523..524
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 552
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 563..564
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 459..515
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 589 AA; 65093 MW; 28ACD5DE82B395F9 CRC64;
MASVGALKFL LFQVLWLWNF LPSCQGDKQW HEKSYPFIRN ASSFSSPSIS TTTSSNVYDY
IIVGGGTAGC PLAATLSQKF NVLMLERGGV PFTNPNVSYL ENFHITLADV SPTSASQFFV
SSDGVYNSRA RILGGGSSIN AGFYTRADPR FIKKVGWDIN LVNQSYPWIE NQIVHRPKFS
AYQRAVRDSL LDSGVSPFNG FTYDHLYGTK VGGTIFDKYG RRHTAAELLA SGNHEKLTVL
VYATVQKIVF DTKGKKPKAV GVIFQDENGK QHEAVLANDR HSEVIMSSGA IGTPQLLMLS
GIGPKEQLQK FNIPVILDNH FVGKGMVDNP MNTMFVPSER PVHQSLIETV GITKMGVYIE
ASSGFSQSND SIHCHHGIVS AEIGQLSTIP PKQRSPEAIK EFIKNKKDLP IEAFKGGFIL
SKVANPWSVG ELKLVNTNVN GNPSVAFNYF SHPYDLERCV KGIRLAIKVV QSKHFTNYTL
CDRKTSEELL NLTVKANVNF IPKHAKDTKS LKQFCKDTVI TIWHYHGGCH VGKVVNPDYM
VLGVDRLRVV DGSTFDESPG TNPQATVMMM GRYMGLKILR DRLGKLAGI
//
