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Database: UniProt
Entry: A0A023BD60_GRENI
LinkDB: A0A023BD60_GRENI
Original site: A0A023BD60_GRENI 
ID   A0A023BD60_GRENI        Unreviewed;       327 AA.
AC   A0A023BD60;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00016495};
GN   ORFNames=GNI_006870 {ECO:0000313|EMBL:EZG87449.1};
OS   Gregarina niphandrodes (Septate eugregarine).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Gregarinasina;
OC   Eugregarinorida; Gregarinidae; Gregarina.
OX   NCBI_TaxID=110365 {ECO:0000313|EMBL:EZG87449.1, ECO:0000313|Proteomes:UP000019763};
RN   [1] {ECO:0000313|EMBL:EZG87449.1, ECO:0000313|Proteomes:UP000019763}
RP   NUCLEOTIDE SEQUENCE.
RA   Omoto C.K., Sibley D., Venepally P., Hadjithomas M., Karamycheva S.,
RA   Brunk B., Roos D., Caler E., Lorenzi H.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001763};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|RuleBase:RU003369}.
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:EZG87449.1}.
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DR   EMBL; AFNH02000052; EZG87449.1; -; Genomic_DNA.
DR   RefSeq; XP_011128654.1; XM_011130352.1.
DR   AlphaFoldDB; A0A023BD60; -.
DR   EnsemblProtists; EZG87449; EZG87449; GNI_006870.
DR   GeneID; 22910517; -.
DR   VEuPathDB; CryptoDB:GNI_006870; -.
DR   eggNOG; KOG1495; Eukaryota.
DR   OMA; HFSTIVG; -.
DR   OrthoDB; 5059897at2759; -.
DR   Proteomes; UP000019763; Unassembled WGS sequence.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:RHEA.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd01339; LDH-like_MDH; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF34; L-LACTATE DEHYDROGENASE; 1.
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; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369,
KW   ECO:0000313|EMBL:EZG87449.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019763}.
FT   DOMAIN          8..151
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          156..312
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         13..18
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         104
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         127..129
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   327 AA;  34641 MW;  716819E5BBAE4EDD CRC64;
     MATRFSPKIA LVGSGMIGGT VGLLSGLSSL SNNIVFLDVV EGMPAGKALD LAQATTCQDI
     QCTSTGCSDL SENSEGLKDA DIVIVTAGFP RKPGMSRDDL LSKNAEVISN VGRAIGKQCP
     KAFVICITNP LDVMVSLLQK VSGLPTNRVV GMAGLLDSSR FRYFLAEALK VSVKDVHTMV
     LGGHGDAMVP VLSATSVNGI PLFTIIEMGM ITQKQVDDIV ERTRQGGGEI VALLKMGSAF
     VAPAVCALSM VQAYLRNERR IIPCCAYIDG KYGLKATYGG VPCIIGSNGV EEVLDLKLAG
     QEKEMFIKSM KDVEDLRANC RKLGFEA
//
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