ID   LDH_PETMA               Reviewed;         334 AA.
AC   P33571;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=L-lactate dehydrogenase;
DE            Short=LDH;
DE            EC=1.1.1.27;
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1542673; DOI=10.1073/pnas.89.5.1799;
RA   Stock D.W., Whitt G.S.;
RT   "Evolutionary implications of the cDNA sequence of the single lactate
RT   dehydrogenase of a lamprey.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:1799-1803(1992).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000305}.
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DR   EMBL; M74064; AAA49267.1; -; mRNA.
DR   PIR; A38231; A38231.
DR   AlphaFoldDB; P33571; -.
DR   SMR; P33571; -.
DR   STRING; 7757.ENSPMAP00000002676; -.
DR   Ensembl; ENSPMAT00000002689; ENSPMAP00000002676; ENSPMAG00000002438.
DR   GeneTree; ENSGT00940000153525; -.
DR   HOGENOM; CLU_045401_0_2_1; -.
DR   OMA; ASCAEYI; -.
DR   TreeFam; TF314963; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000245300; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_00488; Lactate_dehydrog; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR011304; L-lactate_DH.
DR   InterPro; IPR018177; L-lactate_DH_AS.
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; 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; TIGR01771; L-LDH-NAD; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..334
FT                   /note="L-lactate dehydrogenase"
FT                   /id="PRO_0000168488"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         31..59
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   334 AA;  36432 MW;  E8E4245150EA5113 CRC64;
     MASTKGKLIH EMVPSKERDP PHSKVTIVGV GQVGMAAAIS VLLRDLADEL ALVDVVEDRL
     KGEMMDLLHG SLFLKTAKIV ADKDYSVTAG SRLVVVTAGA RQQEGESRLN LVQRNVNIFK
     FIIPNIVKYS PNCILLVVSN PVDILTYVAW KLSGLPKHRV IGSGCNLDSA RFRYLMSERL
     GVNSASCHGW IIGEHGDSSV PVWSGVNVAG VGLQSLNPDI GTPKDGEDWK SVHKQVVDSA
     YEVIKLKGYT SWAIGLSVAD LAETILKNLR RVHPVSTHCK GQHGVHDDVF LSLPCVLGSE
     GITDIINQTL KKEEEAQVQK SAETLWNVQK ELTF