ID MDHM_CAEEL Reviewed; 341 AA. AC O02640; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Malate dehydrogenase, mitochondrial {ECO:0000303|PubMed:34619358}; DE EC=1.1.1.37 {ECO:0000255|PROSITE-ProRule:PRU10004, ECO:0000269|PubMed:34619358}; DE Flags: Precursor; GN Name=mdh-2 {ECO:0000303|PubMed:34619358, GN ECO:0000312|WormBase:F20H11.3}; GN ORFNames=F20H11.3 {ECO:0000312|WormBase:F20H11.3}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=34619358; DOI=10.1016/j.bbapap.2021.140722; RA Thomas M.J., Cassidy E.R., Robinson D.S., Walstrom K.M.; RT "Kinetic characterization and thermostability of C. elegans cytoplasmic and RT mitochondrial malate dehydrogenases."; RL Biochim. Biophys. Acta 1870:140722-140722(2021). CC -!- FUNCTION: Catalyzes the reversible conversion of (S)-malate to CC oxaloacetate in the citric acid cycle. {ECO:0000269|PubMed:34619358}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; CC Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10004, CC ECO:0000269|PubMed:34619358}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=52 uM for oxaloacetate (at 24 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:34619358}; CC KM=42 uM for oxaloacetate (at 24 degrees Celsius and pH 7.5, CC endogenous protein) {ECO:0000269|PubMed:34619358}; CC KM=107 uM for NADH (at 24 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:34619358}; CC Note=kcat is 460 sec(-1) with NADH as substrate (at 24 degrees CC Celsius and pH 7.5).; CC pH dependence: CC Optimum pH is between 6-8.5. {ECO:0000269|PubMed:34619358}; CC Temperature dependence: CC Optimum temperature is 35 degrees Celsius. CC {ECO:0000269|PubMed:34619358}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P40926}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000250|UniProtKB:P04636}. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284603; CCD69776.1; -; Genomic_DNA. DR PIR; C88486; C88486. DR RefSeq; NP_498457.1; NM_066056.5. DR AlphaFoldDB; O02640; -. DR SMR; O02640; -. DR BioGRID; 41153; 41. DR STRING; 6239.F20H11.3.1; -. DR EPD; O02640; -. DR PaxDb; 6239-F20H11-3; -. DR PeptideAtlas; O02640; -. DR EnsemblMetazoa; F20H11.3.1; F20H11.3.1; WBGene00003162. DR GeneID; 175936; -. DR KEGG; cel:CELE_F20H11.3; -. DR UCSC; F20H11.3.1; c. elegans. DR AGR; WB:WBGene00003162; -. DR WormBase; F20H11.3; CE09512; WBGene00003162; mdh-2. DR eggNOG; KOG1494; Eukaryota. DR GeneTree; ENSGT00390000016686; -. DR HOGENOM; CLU_047181_1_0_1; -. DR InParanoid; O02640; -. DR OMA; SHMDTPA; -. DR OrthoDB; 5059897at2759; -. DR PhylomeDB; O02640; -. DR Reactome; R-CEL-70263; Gluconeogenesis. DR Reactome; R-CEL-71403; Citric acid cycle (TCA cycle). DR PRO; PR:O02640; -. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00003162; Expressed in adult organism and 4 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; HDA:WormBase. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IDA:UniProtKB. DR GO; GO:0006108; P:malate metabolic process; IDA:UniProtKB. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 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; IPR001252; Malate_DH_AS. DR InterPro; IPR010097; Malate_DH_type1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01772; MDH_euk_gproteo; 1. DR PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1. DR PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00068; MDH; 1. PE 1: Evidence at protein level; KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; Transit peptide; KW Tricarboxylic acid cycle. FT TRANSIT 1..? FT /note="Mitochondrion" FT CHAIN ?..341 FT /note="Malate dehydrogenase, mitochondrial" FT /id="PRO_0000018632" FT ACT_SITE 204 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P00346" FT BINDING 35..41 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 61 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 108 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 114 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 121 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 144..146 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 146 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 180 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 255 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" SQ SEQUENCE 341 AA; 35120 MW; 7515F9C1727AEFB5 CRC64; MSLPAKTLVQ AAANSGLRAV SVRHSSQAPK VALLGAAGGI GQPLGLLLKQ DPLVAHLALY DVVNTPGVAA DLSHIDSNAK VTAHTGPKEL YAAVENADVI VIPAGVPRKP GMTRDDLFNT NAGIVRDLAA VIAKASPKAL IAIITNPVNS TVPIASEVLK KAGVYDPKRV FGVTTLDVVR SQAFVSELKG HDASKTVVPV VGGHAGITII PLLSQVKPST KFSEEEISKL TPRIQDAGTE VVNAKAGAGS ATLSMALAGA RFANALVRGI KGEKNVQCAY VASDAVKGVE YFSTPVELGP NGVEKILGVG KVSAYEQKLI DASVPELNKN IAKGVAFVKG N //