ID B3RNL5_TRIAD Unreviewed; 556 AA.
AC B3RNL5;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIADDRAFT_53208 {ECO:0000313|EMBL:EDV28039.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV28039.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV28039.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV28039.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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; DS985242; EDV28039.1; -; Genomic_DNA.
DR RefSeq; XP_002109873.1; XM_002109837.1.
DR AlphaFoldDB; B3RNL5; -.
DR STRING; 10228.B3RNL5; -.
DR EnsemblMetazoa; TriadT53208; TriadP53208; TriadG53208.
DR GeneID; 6750527; -.
DR KEGG; tad:TRIADDRAFT_53208; -.
DR CTD; 6750527; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_7_0_1; -.
DR InParanoid; B3RNL5; -.
DR OMA; ANLEYHV; -.
DR OrthoDB; 3382025at2759; -.
DR PhylomeDB; B3RNL5; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 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; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT DOMAIN 20..295
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 409..551
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 90..93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 220
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 556 AA; 61203 MW; 08CE5BE688DB50A5 CRC64;
MSYSYFTKRS AITDNFLPAY DYIVIGGGSA GCVIANRLSE DLKTTVLLLE AGPSHEKKSA
LKVPAKTIDL HNDPNFDWSY KVLGGCSSIN FMVYIRGCKG DYDTWQEMGA QGWNFESVLP
YFIKSENNIR PEFRKDPAHG VGGPVTVTDP SFTTPVTDAF VKAGVKLGNK ECDINSGVKN
GFDLGQLVIK NGQRQSTAAS YLTSKVLRRR NLAIGVNCLV RKVVFKENKA VGVEFSKNDK
IITISCNSEV IVCGGVIGSP QILLLSGVGP KEDLEKLEIP VVANLPVGRN MQDHNAISIS
SLTKDLQNST LNLKSATKLS SILKYLFKGK GVIASSGYLA SGFVNAVDDS DALPWPDTQI
HLFGYGVLSD KFYYENLGYN KEKHFPLFIG NSMAQDQEGF TLVPVLLHPK SRGTVKLRST
DPAEYPDIDP KYYDDPDDLT AMAKIVQYAI KLLETEPLCS YIKEVLRYKI DSSHEYNSIE
YWKDVIRVYG MDCFHPVGTC KMGAVDDPTT VVDSDLRIHG LDGIRVADAS IMPCIVSGNT
NAACMMIGSK AFFLWR
//