MDHC_CAEEL
ID MDHC_CAEEL Reviewed; 336 AA.
AC Q9UAV5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Malate dehydrogenase, cytoplasmic {ECO:0000303|PubMed:34619358};
DE EC=1.1.1.37 {ECO:0000269|PubMed:34619358};
GN Name=mdh-1 {ECO:0000303|PubMed:34619358, ECO:0000312|WormBase:F46E10.10};
GN ORFNames=F46E10.10 {ECO:0000312|WormBase:F46E10.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
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 cytoplasm where oxaloacetate is used for
CC gluconeogenesis. {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:0000269|PubMed:34619358};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=54 uM for oxaloacetate (at 24 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:34619358};
CC KM=50 uM for oxaloacetate (at 24 degrees Celsius and pH 7.5,
CC endogenous protein) {ECO:0000269|PubMed:34619358};
CC KM=61 uM for NADH (at 24 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:34619358};
CC Note=kcat is 350 sec(-1) with NADH as substrate (at 24 degrees
CC Celsius and pH 7.5). {ECO:0000269|PubMed:34619358};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:34619358};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11708}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000305}.
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DR EMBL; BX284605; CCD71316.1; -; Genomic_DNA.
DR PIR; T33966; T33966.
DR RefSeq; NP_504656.1; NM_072255.3.
DR AlphaFoldDB; Q9UAV5; -.
DR SMR; Q9UAV5; -.
DR DIP; DIP-25233N; -.
DR STRING; 6239.F46E10.10a; -.
DR EPD; Q9UAV5; -.
DR PaxDb; Q9UAV5; -.
DR PeptideAtlas; Q9UAV5; -.
DR EnsemblMetazoa; F46E10.10.1; F46E10.10.1; WBGene00018491.
DR GeneID; 179041; -.
DR KEGG; cel:CELE_F46E10.10; -.
DR UCSC; F46E10.10c.1; c. elegans.
DR CTD; 179041; -.
DR WormBase; F46E10.10; CE20820; WBGene00018491; mdh-1.
DR eggNOG; KOG1496; Eukaryota.
DR GeneTree; ENSGT00530000063410; -.
DR HOGENOM; CLU_040727_2_0_1; -.
DR OMA; TKGMERG; -.
DR OrthoDB; 1118998at2759; -.
DR PhylomeDB; Q9UAV5; -.
DR Reactome; R-CEL-70263; Gluconeogenesis.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00018491; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0006108; P:malate metabolic process; IDA:UniProtKB.
DR GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd01336; MDH_cytoplasmic_cytosolic; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_01517; Malate_dehydrog_2; 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; IPR011274; Malate_DH_NAD-dep_euk.
DR InterPro; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23382; PTHR23382; 1.
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; TIGR01759; MalateDH-SF1; 1.
DR TIGRFAMs; TIGR01758; MDH_euk_cyt; 1.
DR PROSITE; PS00068; MDH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..336
FT /note="Malate dehydrogenase, cytoplasmic"
FT /id="PRO_0000454789"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000102-1"
FT BINDING 11..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000102-2"
FT BINDING 105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 129..131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000102-2"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000102-2"
SQ SEQUENCE 336 AA; 35806 MW; F1CB2FED796E0024 CRC64;
MSAPLRVLVT GAAGQIGYSI VIRIADGTVF GKEQPVELVL LDVPQCSNIL EGVVFELQDC
ALPTLFSVVA VTDEKSAFTG IDYAFLVGAM PRREGMERKD LLAANVKIFK SQGKALAEYA
KPTTKVIVVG NPANTNAFIA AKYAAGKIPA KNFSAMTRLD HNRALAQLAL KTGTTIGNVK
NVIIWGNHSG TQFPDVTHAT VNKNGTETDA YAAVGDNAFL QGPFIATVQK RGGVIIEKRK
LSSAMSAAKA ACDHIHDWHF GTKAGQFVSM AVPSDGSYGI PQGLIFSFPV TIEGGEWKIV
QGLSFDDFAK GKIAATTKEL EEERDDALKA CDDANI
