ID V4ZH75_TOXGV Unreviewed; 759 AA.
AC V4ZH75;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:ESS31667.1};
GN ORFNames=TGVEG_243655 {ECO:0000313|EMBL:ESS31667.1};
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS31667.1, ECO:0000313|Proteomes:UP000002226};
RN [1] {ECO:0000313|Proteomes:UP000002226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESS31667.1}.
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DR EMBL; AAYL02000165; ESS31667.1; -; Genomic_DNA.
DR AlphaFoldDB; V4ZH75; -.
DR STRING; 432359.V4ZH75; -.
DR PaxDb; 5811-TGME49_043650; -.
DR EnsemblProtists; ESS31667; ESS31667; TGVEG_243655.
DR VEuPathDB; ToxoDB:TGVEG_243655; -.
DR eggNOG; KOG1238; Eukaryota.
DR OMA; AEPACKD; -.
DR Proteomes; UP000002226; Partially assembled 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; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002226}.
FT DOMAIN 179..193
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 443..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 83611 MW; 39CD7DCEDAD45F9C CRC64;
MPQDTQYVSR LAMSLQDEGY KPLFPSDERA KDFNCPRSGL GCTAKILPGH VWGGVTVFDK
EKNFFRNAAD VFVYEAPGVP AHPDRLLVKT EQFVERVLFA TSKVSQPRAV CVSYRPSSAE
DMAPIGLDAP PPQKTGESRG LLSSLLSYAL QMLEWIWPND SSLEIACLRG QGEIILSAGA
VHTPLLLFRS GVGPQEQLQE IGVPAVAVVE ELGRNLSDRI LIPIQMFQKD NKRKEDRNPR
VCQVLGARHQ GPHCDGVGIN ERTLKCSLLT TEELSGPNVI HGLLWASHLL LPPSWRDHPA
AHAVFNFVRF CEGKMKFQGT LQYPPACMFV EGLLDCLDRS ISLFYFTTEP KSRGYIRQHK
DGRVEVEANY LKNEQDLFDA TRGVQSLIQQ VNGGRFADIV EPLQPGSCPV LMLYTVVSLF
LDFAQAADLP QYEKQLLSVR RHSTDLQTHH HEQARATMPS ASEDELPFLR LIQNLTESRG
GLKNEKQPSA IRAAANDPER SEGAAAHGTA AQPAEGFEED LGKVFKDREK LKRLFENGSA
QQRRRQTNML PETTKQSSQK KDELAPQSRV CAADAEPACK DGPIHSDVYT TTCSAHDIFT
KRYGSSACSS SPDASTAQAE SPESFISWQA GLAEAGIQQF FGERLPPGSG QWAATYPPVL
PQVDDPEAVA AFAVTYMTSI WHLAGTAAVG HVVDHEFRVM GTKNLSIADA SVLNQMTRLN
PTATLLTLGR YIGLLKVKSS ERNTNNDRKS GEHGRKGGL
//