ID   LDH_MAIZE               Reviewed;         354 AA.
AC   P29038;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=L-lactate dehydrogenase;
DE            Short=LDH;
DE            EC=1.1.1.27;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RX   PubMed=1627781; DOI=10.1007/bf00026795;
RA   Good A.G., Paetkau D.H.;
RT   "Identification and characterization of a hypoxically induced maize lactate
RT   dehydrogenase gene.";
RL   Plant Mol. Biol. 19:693-697(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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10002};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- INDUCTION: By hypoxia.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000305}.
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DR   EMBL; Z11754; CAA77808.1; -; Genomic_DNA.
DR   PIR; S22492; S22492.
DR   AlphaFoldDB; P29038; -.
DR   SMR; P29038; -.
DR   STRING; 4577.GRMZM2G128929_P01; -.
DR   PaxDb; P29038; -.
DR   PRIDE; P29038; -.
DR   MaizeGDB; 65834; -.
DR   eggNOG; KOG1495; Eukaryota.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P29038; differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.110.10; -; 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   NAD; Oxidoreductase; Reference proteome; Stress response.
FT   CHAIN           1..354
FT                   /note="L-lactate dehydrogenase"
FT                   /id="PRO_0000168491"
FT   REGION          302..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        214
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10002"
FT   BINDING         73..78
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  38551 MW;  4F903F7C3E203FC2 CRC64;
     MKKATSLSEL GFDAGDASSG FFRPVSGDSS TPTSQHHRRR LTKVSVIGAG NVGMAIAQTI
     LTRDLADEIA LVDAVPDKLR GEMLDLQHAA AFLPRTRLVS GTDMSVTRGS DLVIVTAGAR
     QIQGETRLDL LQRNVALFRK IVPPLAEQSH DALLLVVSNP VDVLTYVAWK LSGFPASRVI
     GSGTNLDSSR FRFLLAEHLD VNAQDVQAYM VGEHGDSSVA VWSSVSVAGM PVLKSLQESH
     RCFDEEALEG IRRAVVDSAY EVISLKGYTS WAIGYSVASL AASLLRDQRR IHPVSVLARG
     FHGIPDGTTS SSACPPRRPR RRPGRREMEL TEEEAKRLRR SAKTIWENCQ LLGL