ID Q4DGI4_TRYCC Unreviewed; 614 AA.
AC Q4DGI4;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase (FAD-dependent), putative {ECO:0000313|EMBL:EAN91630.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:EAN91630.1};
GN ORFNames=Tc00.1047053511423.70 {ECO:0000313|EMBL:EAN91630.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN91630.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN91630.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN91630.1,
RC ECO:0000313|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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:EAN91630.1}.
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DR EMBL; AAHK01000507; EAN91630.1; -; Genomic_DNA.
DR RefSeq; XP_813481.1; XM_808388.1.
DR AlphaFoldDB; Q4DGI4; -.
DR SMR; Q4DGI4; -.
DR STRING; 353153.Q4DGI4; -.
DR PaxDb; 353153-Q4DGI4; -.
DR EnsemblProtists; EAN91630; EAN91630; Tc00.1047053511423.70.
DR GeneID; 3544860; -.
DR KEGG; tcr:511423.70; -.
DR eggNOG; KOG0042; Eukaryota.
DR InParanoid; Q4DGI4; -.
DR OMA; ETTWRNV; -.
DR OrthoDB; 152269at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR031656; DAO_C.
DR InterPro; IPR038299; DAO_C_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR PANTHER; PTHR11985:SF11; DEHYDROGENASE (FAD-DEPENDENT), PUTATIVE-RELATED; 1.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EAN91630.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002296};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..484
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 546..596
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 614 AA; 66187 MW; 734E49BDEBFF8DB2 CRC64;
MGRRSRRFAA RVAAVGVAFV SGWALYHRWQ LRRSAVVLLP VDTTMNMPQS HAMRLQLLGS
STKKEPFDVL VIGGGATGLY TAVDAAQRGL RVALVDADDF GAGHTGTSPP LIPGAFSYIQ
RALRQRDLLW LRRGVEAWRA LTVWSNVAPG LLENGVSTLV LSCHFLELME LTTAAVIATL
LSTFSGDWRP FRFVRGNVLR NEFQEAGKAM RGGILVEDAF LDGNAASIAL ARTAEALGAV
VLNYASVTSI TNVETTAELK GQANFAVLVN DVSTPNGVGE LAPRAVTVYT RSIVNCAGSW
VDEVKQLVPG NAMDAVPSAV QRHQVRSYLV LPRTAVQTAT PKNVDLLFGA DAFSVAPTSY
SFSSVMMLPW FDGCVLIGPS LSSLFRLPSK SYAVAPTTVL TLAGTKNNNG CDIHDVYISQ
RKHLFRALQV SGVKVDEERV LSCLSSIVPI IASPPRVPLA KDIFMGGCHI SSGKEQPNVV
HVYGGTLGFA RDIAEKALDR LLHDSGAFST AETAALRPCQ TSRLALVGAQ SKDATSDVVS
PVKRIQRIVR EEYAARLLDI VARRKHTAYS SPAEALAALP AIAEIMRCEL GWTAERTKVE
LEMAKAFIRS ISFA
//
