LDH_PLABA
ID LDH_PLABA Reviewed; 316 AA.
AC Q7SI97; Q4Z783;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=L-lactate dehydrogenase;
DE EC=1.1.1.27;
GN ORFNames=PB000185.00.0;
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823;
RN [1] {ECO:0000312|EMBL:CAH93763.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANKA;
RX PubMed=15637271; DOI=10.1126/science.1103717;
RA Hall N., Karras M., Raine J.D., Carlton J.M., Kooij T.W.A., Berriman M.,
RA Florens L., Janssen C.S., Pain A., Christophides G.K., James K.,
RA Rutherford K., Harris B., Harris D., Churcher C.M., Quail M.A., Ormond D.,
RA Doggett J., Trueman H.E., Mendoza J., Bidwell S.L., Rajandream M.A.,
RA Carucci D.J., Yates J.R. III, Kafatos F.C., Janse C.J., Barrell B.G.,
RA Turner C.M.R., Waters A.P., Sinden R.S.;
RT "A comprehensive survey of the Plasmodium life cycle by genomic,
RT transcriptomic, and proteomic analyses.";
RL Science 307:82-86(2005).
RN [2] {ECO:0000305, ECO:0000312|PDB:1OC4}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADP AND OXAMATE,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=12967707; DOI=10.1016/s0166-6851(03)00170-1;
RA Winter V.J., Cameron A., Tranter R., Sessions R.B., Brady R.L.;
RT "Crystal structure of Plasmodium berghei lactate dehydrogenase indicates
RT the unique structural differences of these enzymes are shared across the
RT Plasmodium genus.";
RL Mol. Biochem. Parasitol. 131:1-10(2003).
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 Evidence={ECO:0000269|PubMed:12967707};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for NADH {ECO:0000269|PubMed:12967707};
CC KM=57 uM for pyruvate {ECO:0000269|PubMed:12967707};
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12967707}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000255}.
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DR EMBL; CAAI01000126; CAH93763.1; -; Genomic_DNA.
DR RefSeq; XP_679401.1; XM_674309.1.
DR PDB; 1OC4; X-ray; 2.30 A; A/B=1-316.
DR PDBsum; 1OC4; -.
DR AlphaFoldDB; Q7SI97; -.
DR SMR; Q7SI97; -.
DR STRING; 5821.PBANKA_134010; -.
DR VEuPathDB; PlasmoDB:PBANKA_1340100; -.
DR eggNOG; KOG1495; Eukaryota.
DR HOGENOM; CLU_045401_2_1_1; -.
DR InParanoid; Q7SI97; -.
DR OMA; ASCAEYI; -.
DR SABIO-RK; Q7SI97; -.
DR UniPathway; UPA00554; UER00611.
DR EvolutionaryTrace; Q7SI97; -.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; TAS:UniProtKB.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Pyruvate.
FT CHAIN 1..316
FT /note="L-lactate dehydrogenase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000227537"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:12967707"
FT BINDING 13..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12967707"
FT BINDING 34..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12967707"
FT BINDING 67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12967707"
FT BINDING 79..83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12967707"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12967707"
FT BINDING 125..127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12967707"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12967707"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12967707"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12967707"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1OC4"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1OC4"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 40..55
FT /evidence="ECO:0007829|PDB:1OC4"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:1OC4"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:1OC4"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:1OC4"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1OC4"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1OC4"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 152..167
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1OC4"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 211..222
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 237..251
FT /evidence="ECO:0007829|PDB:1OC4"
FT STRAND 256..266
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:1OC4"
FT STRAND 271..282
FT /evidence="ECO:0007829|PDB:1OC4"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1OC4"
FT HELIX 296..314
FT /evidence="ECO:0007829|PDB:1OC4"
SQ SEQUENCE 316 AA; 34424 MW; 582283BBAF946F26 CRC64;
MAPKAKIVLV GSGMIGGVMA TLIVQKNLGD VVMFDIVKNM PHGKALDTSH TNVMAYSNCK
VSGSNTYDDL KDADVVIVTA GFTKAPGKSD KEWNRDDLLP LNNKIMIEIG GHIKNNCPNA
FIIVVTNPVD VMVQLLHQHS GVPKNKIVGL GGVLDTSRLK YYISQKLNVC PRDVNAHIVG
AHGNKMVLLK RYITVGGIPL QEFINNKKIT DQELDAIFDR TINTALEIVN LHASPYVAPA
AAIIEMAESY IRDLRKVLIC STLLEGQYGH KDIFAGTPLV IGGNGVEQVI ELQLNADEKK
KFDEAVAETS RMKALI
