MDHM_CAEEL
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 03-AUG-2022, entry version 154.
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, 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}.
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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; 39.
DR STRING; 6239.F20H11.3; -.
DR EPD; O02640; -.
DR PaxDb; O02640; -.
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 CTD; 175936; -.
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; MGWTSQA; -.
DR OrthoDB; 976445at2759; -.
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 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; -; 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 Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 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
