ID T1G8W2_HELRO Unreviewed; 643 AA.
AC T1G8W2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN Name=20217509 {ECO:0000313|EnsemblMetazoa:HelroP93524};
GN ORFNames=HELRODRAFT_93524 {ECO:0000313|EMBL:ESO12860.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP93524, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESO12860.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP93524}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; AMQM01000252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB095811; ESO12860.1; -; Genomic_DNA.
DR RefSeq; XP_009009580.1; XM_009011332.1.
DR AlphaFoldDB; T1G8W2; -.
DR STRING; 6412.T1G8W2; -.
DR EnsemblMetazoa; HelroT93524; HelroP93524; HelroG93524.
DR GeneID; 20217509; -.
DR KEGG; hro:HELRODRAFT_93524; -.
DR CTD; 20217509; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_7_0_1; -.
DR InParanoid; T1G8W2; -.
DR OMA; EIMPMAY; -.
DR OrthoDB; 2955079at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000015101};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..146
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT BINDING 129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 643 AA; 71674 MW; 21EB47186D03D7F2 CRC64;
MSIGKYIPAI IVVGIGLTFY RLLGLGDYFV ELIKAKELQK EYDYIIVGGG TAGAVLAARL
ADNKDFNILL VEAGSNPSSN PLVDIPLMAD SIRTPQLDWH HKTVPQKFAC KGHVDQSAII
HSGKGLGGTS NINYMQYLRG SRYDYDGWAL NGAAGWAYKD VLPYFIKSED QQNGEFVRTV
FHGFGGRLAV KDVGPTTMNQ IMGLCFKEIS LKKRDLNGKN QFGWGPTQAT IRNGVRWSTF
KAYLKRYMNA PNLHVVTDTF AEKILFEGKR ADSIVLKHEK KTEVVKAKKE IILTAGTVGT
TKLLLLSGVG PKTHLQKLKI PVVADLPVGE NLQDQVVGDG IEYYTPYPGV SITINMADSL
LSSWAYSLFG TEVTTSLAGM KSSPRFREAT AYIRLRHQPP NIKYPLLALH IAANPQAYEA
TSKLHTAHDL FQTWAEIHGK PLSREGFTIF PVLLHPRSRG TIRLNTTNPE DPPLIDPNYL
SEEIDIKILT EGFQFARRLL HTQVMKDWEF KLTNRLLPEC QKYGNYTNAY VECHLRHITI
PGGNLVGTCK MGALNDPRAV VDPILRVRGL KGLRVADASI IPTSMSADTY ATQVMIAEKA
ADFILEKDTV RSIKEYFKHL IESRHKKIMD DEEAEEAHTA KKS
//
