LDH_TOXGO
ID LDH_TOXGO Reviewed; 326 AA.
AC Q27797;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=L-lactate dehydrogenase;
DE Short=LDH;
DE EC=1.1.1.27;
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 50611 / Me49;
RX PubMed=8577343; DOI=10.1016/0166-6851(95)00124-j;
RA Yang S., Parmley S.F.;
RT "A bradyzoite stage-specifically expressed gene of Toxoplasma gondii
RT encodes a polypeptide homologous to lactate dehydrogenase.";
RL Mol. Biochem. Parasitol. 73:291-294(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27;
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
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DR EMBL; U23207; AAC46863.1; -; mRNA.
DR PDB; 1SOV; X-ray; 1.90 A; A/B=1-326.
DR PDB; 1SOW; X-ray; 1.90 A; A/B=1-326.
DR PDB; 3CZM; X-ray; 2.30 A; A/B=1-326.
DR PDBsum; 1SOV; -.
DR PDBsum; 1SOW; -.
DR PDBsum; 3CZM; -.
DR AlphaFoldDB; Q27797; -.
DR SMR; Q27797; -.
DR VEuPathDB; ToxoDB:TGARI_291040; -.
DR VEuPathDB; ToxoDB:TGCAST_291040; -.
DR VEuPathDB; ToxoDB:TGCOUG_291040; -.
DR VEuPathDB; ToxoDB:TGDOM2_291040; -.
DR VEuPathDB; ToxoDB:TGFOU_291040; -.
DR VEuPathDB; ToxoDB:TGGT1_291040; -.
DR VEuPathDB; ToxoDB:TGMAS_291040; -.
DR VEuPathDB; ToxoDB:TGME49_291040; -.
DR VEuPathDB; ToxoDB:TGP89_291040; -.
DR VEuPathDB; ToxoDB:TGPRC2_291040; -.
DR VEuPathDB; ToxoDB:TGRH88_015400; -.
DR VEuPathDB; ToxoDB:TGRUB_291040; -.
DR VEuPathDB; ToxoDB:TGVAND_291040; -.
DR VEuPathDB; ToxoDB:TGVEG_291040; -.
DR BRENDA; 1.1.1.27; 6411.
DR SABIO-RK; Q27797; -.
DR UniPathway; UPA00554; UER00611.
DR EvolutionaryTrace; Q27797; -.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd01339; LDH-like_MDH; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR011275; Malate_DH_type3.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase.
FT CHAIN 1..326
FT /note="L-lactate dehydrogenase"
FT /id="PRO_0000168497"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 39..60
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:1SOV"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1SOV"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1SOW"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:1SOV"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1SOV"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1SOW"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 103..120
FT /evidence="ECO:0007829|PDB:1SOV"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1SOV"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 156..171
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1SOV"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 215..236
FT /evidence="ECO:0007829|PDB:1SOV"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 243..257
FT /evidence="ECO:0007829|PDB:1SOV"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:1SOV"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:1SOV"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:1SOV"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:1SOV"
FT HELIX 302..323
FT /evidence="ECO:0007829|PDB:1SOV"
SQ SEQUENCE 326 AA; 35307 MW; E692C95A81FC031E CRC64;
MTGTVSRRKK IAMIGSGMIG GTMGYLCVLR ELADVVLFDV VTGMPEGKAL DDSQATSIAD
TNVSVTSANQ YEKIAGSDVV IITAGLTKVP GKSDKEWSRN DLLPFNAKII REVAQGVKKY
CPLAFVIVVT NPLDCMVKCF HEASGLPKNM VCGMANVLDS ARFRRFIADQ LEISPRDIQA
TVIGTHGDHM LPLARYVTVS GFPLREFIKK GKMTEAKLAE IVERTKKAGG EIVRLLGQGS
AYYAPALSAI TMAQAFLKDE KRVLPCSVYC QGEYGLHDMF IGLPAVIGGG GIEQVIELEL
THEEQECFRK SVDDVVELNK SLAALG
