ID G0V1L0_TRYCI Unreviewed; 581 AA.
AC G0V1L0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Uncharacterized protein TCIL3000_11_10030 {ECO:0000313|EMBL:CCC95531.1};
GN ORFNames=TCIL3000_11_10030 {ECO:0000313|EMBL:CCC95531.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC95531.1};
RN [1] {ECO:0000313|EMBL:CCC95531.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCC95531.1};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; HE575324; CCC95531.1; -; Genomic_DNA.
DR AlphaFoldDB; G0V1L0; -.
DR VEuPathDB; TriTrypDB:TcIL3000.11.10030; -.
DR OrthoDB; 3382025at2759; -.
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; 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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 302..316
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 581 AA; 62727 MW; 0235EBAA6092BE28 CRC64;
MNFSWITNTL YLSSVYRHIS RVICIFGLNS LCAYSIRKGM SCKATAFDIV VLGAGSAGCA
AARSIALQHP GAAVCLIEQG CREPPPLTMR VPLLSPLIGS FRNTRRFLRF YRGIPEDCLG
GRQLHYMKGR GLGGSSWCND MKYLRGTAED YNSWGDAAWE MEQVLPFFKA LECNSRIGAS
EHHGDSGPLV VTDPPAANVN SELNIRWFEA CEALGIPQIS DFNSGTSDGF SCFQSHINKG
ARVDVFDSLL ESERHLLPNL TIFSDTRANR IVFDKSRAVG IEVIKERSVT VLPIHRLVLC
LGALESPALL LRSGIGPRGD VAELPGVGQN LIQSCSAVVV FRISRSSNLH SKSLSFSNGA
YLRYQWREYT EERSGIFASF AEAGAFVRST PSAARPDLSL TFYPTPNVRW CGWRPFDGFA
VRVTHHYPEA RGEVVLGDGG GSRSSVGSDG EVQIASRMLS ARHDVQCMDE GLRWVGSLCS
RGGARFQQPA PFAPLGTSLQ HPATGLSTQR STAAFLAQYA ESTGDIFGTC ALGTVVDGTL
RVRGVEGIHV ADASVVPVPT CGSSSVIGAV IGSRVGSFLA K
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