ID A0A0L0D3Z8_THETB Unreviewed; 632 AA.
AC A0A0L0D3Z8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:KNC46816.1};
GN ORFNames=AMSG_03247 {ECO:0000313|EMBL:KNC46816.1};
OS Thecamonas trahens ATCC 50062.
OC Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC46816.1, ECO:0000313|Proteomes:UP000054408};
RN [1] {ECO:0000313|EMBL:KNC46816.1, ECO:0000313|Proteomes:UP000054408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC46816.1,
RC ECO:0000313|Proteomes:UP000054408};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL Submitted (MAY-2010) 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, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; GL349444; KNC46816.1; -; Genomic_DNA.
DR RefSeq; XP_013760091.1; XM_013904637.1.
DR AlphaFoldDB; A0A0L0D3Z8; -.
DR STRING; 461836.A0A0L0D3Z8; -.
DR EnsemblProtists; KNC46816; KNC46816; AMSG_03247.
DR GeneID; 25562861; -.
DR eggNOG; KOG1238; Eukaryota.
DR OMA; NYPWIHI; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000054408; 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; 3.50.50.60; 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.
DR PROSITE; PS00624; GMC_OXRED_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054408};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..632
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005537097"
FT DOMAIN 121..144
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 319..333
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 103..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131..134
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 268
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 632 AA; 66342 MW; FD555C6CA5C75CC2 CRC64;
MTCRFWTSAV LVVLAAAAAY RVLVPPPAEF AHTPLLDEYD YVVVGGGSAG AVAAARLAEG
APDARVLLLE AGPSDSAMME VAIPAGCSLL QRTKLDWQFT TQPQAASHGS MHERRSRWPR
GKTLGGSSSI NYMVYVRGAQ DDYDKLWGVS GWSFADVLPF FRKSENYVAR PLAANETHRA
TGGPLTVSKP QTSSPLVDAF IASGKALGLA RNEDYNGAGG MMGIAHCDLT IKDGVRASSA
AAFLRPALAR AAAASASGVF HVRTFAHVTR VVTETDAASG KVRAVGVEFA DTADSDGVAS
EDSPRRVVRA TTEVVLSAGA VGSPHVLMLS GIGPEDVLAA AGIETVVDLP GVGRNLRDHL
MVPVRFPTKD KASGHLITKK RAESLTTLLK YLVFSGGLLT TNGLEGTAFY STGTSDHLPA
SVPDVQIHMI ATGGSDVEAA NIGTKPEFVA QGVIDDPDRW QAGGINFLPI ILHPKSRGAI
TLNSSSPFDP PLIQPNYLAE QADVDLLVAA VHDTLKLAAD EAYAEWIDAS SPTTSPLYES
APDGAAAGVS YWEWHVRNFA VTVYHPVGTA KMGEPGAAGT VVDPQLRVVG VDGLRVADAS
IMPTLISGNT NAPCIMIGER VADFILSSLQ GR
//
