ID Q9BKE1_TOXGO Unreviewed; 592 AA.
AC Q9BKE1;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:AAK20421.1};
DE Flags: Fragment;
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811 {ECO:0000313|EMBL:AAK20421.1};
RN [1] {ECO:0000313|EMBL:AAK20421.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11230543;
RA Fast N.M., Kissinger J.C., Roos D.S., Keeling P.J.;
RT "Nuclear-encoded, plastid-targeted genes suggest a single common origin for
RT apicomplexan and dinoflagellate plastids.";
RL Mol. Biol. Evol. 18:418-426(2001).
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR EMBL; AF265362; AAK20421.1; -; mRNA.
DR AlphaFoldDB; Q9BKE1; -.
DR VEuPathDB; ToxoDB:TGARI_269190; -.
DR VEuPathDB; ToxoDB:TGCAST_269190; -.
DR VEuPathDB; ToxoDB:TGCOUG_269190; -.
DR VEuPathDB; ToxoDB:TGDOM2_269190; -.
DR VEuPathDB; ToxoDB:TGFOU_269190; -.
DR VEuPathDB; ToxoDB:TGGT1_269190; -.
DR VEuPathDB; ToxoDB:TGMAS_269190; -.
DR VEuPathDB; ToxoDB:TGME49_269190; -.
DR VEuPathDB; ToxoDB:TGP89_269190; -.
DR VEuPathDB; ToxoDB:TGPRC2_269190; -.
DR VEuPathDB; ToxoDB:TGRH88_082060; -.
DR VEuPathDB; ToxoDB:TGRUB_269190; -.
DR VEuPathDB; ToxoDB:TGVAND_269190; -.
DR VEuPathDB; ToxoDB:TGVEG_269190; -.
DR HOGENOM; CLU_030140_0_3_1; -.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01534; GAPDH-I; 1.
DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 2: Evidence at transcript level;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 243..395
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT REGION 188..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAK20421.1"
SQ SEQUENCE 592 AA; 62129 MW; DE8F6AA8E6B2E12D CRC64;
PVLLCMQTRI CVVSTRGASS RSNRVGTKVL QRCLLDEAYL ALLTKTPDFC AAAPAEAETG
LGNSAAQATG TPVSPFAGAA PLEPMAAVTE GEIEAVALDL LQESGVDGPA VLEHMARDGR
GSASDLCSLV QTLATELLQT ERDPRCAAAP TSEDRENIAL TTEALLTSAF GFLGPASPSA
TAATAATVAS GTPQNARSAS IRSHRRNSFA PTGKRAVAPV PRVSPTGLFG LLGSSSEKAS
APIRLGINGM GRIGRLVFRI AMSRPDVAVT HINCSMDPAY IAYMLKYDSV HGKFDGEIVP
TETSLIVNGQ EVTISNTRDP EEIPWADKGA DYVCESTGVF CTTEAAAKHV NRPGGAKHAI
ISAPAKDETT PTLVVGVNAE QDYESSMKVV SCASCTTNGL APLVKVIDEN FGLVEGLMTT
VHAATGTQKV VDGTSKKDWR GGRAAAGNII PSATGAAKAV ARCLPHMKGK LTGMAFRVPT
LDVSVVDLTC RLNKSTTYEE IKKAVREASE TYMRGIIGYT EEPIVSQDIV GSQCSTVFDA
NAGIMLNPNF VKLVSWYDNE YAYSARLVDL IAVMAAKDGV VSPGTGLDRR PF
//
