ID MDHC_DICDI Reviewed; 333 AA. AC Q54VM2; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=Probable malate dehydrogenase 3; DE EC=1.1.1.37; GN Name=mdhC; ORFNames=DDB_G0280255; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. CC {ECO:0000250}. 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 -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 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; AAFI02000035; EAL67354.1; -; Genomic_DNA. DR RefSeq; XP_641333.1; XM_636241.1. DR AlphaFoldDB; Q54VM2; -. DR SMR; Q54VM2; -. DR STRING; 44689.Q54VM2; -. DR PaxDb; 44689-DDB0230187; -. DR EnsemblProtists; EAL67354; EAL67354; DDB_G0280255. DR GeneID; 8622467; -. DR KEGG; ddi:DDB_G0280255; -. DR dictyBase; DDB_G0280255; mdhC. DR eggNOG; KOG1496; Eukaryota. DR HOGENOM; CLU_040727_2_0_1; -. DR InParanoid; Q54VM2; -. DR OMA; GMIGSNM; -. DR PhylomeDB; Q54VM2; -. DR PRO; PR:Q54VM2; -. DR Proteomes; UP000002195; Chromosome 3. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central. 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; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR01759; MalateDH-SF1; 1. DR NCBIfam; TIGR01758; MDH_euk_cyt; 1. DR PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1. DR PANTHER; PTHR23382:SF25; MALATE DEHYDROGENASE 3-RELATED; 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 3: Inferred from homology; KW NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1..333 FT /note="Probable malate dehydrogenase 3" FT /id="PRO_0000312366" FT ACT_SITE 188 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 12..18 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 93 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 106 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 113 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 130..132 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 132 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 163 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 333 AA; 35986 MW; B98891A299AB53FF CRC64; MSNEVINVLI TGAAGQIAYS LIFNVCKGDM FGLDQRIKLH LLDIPQMVDS LKGIVMEIQD GAYPLIADTV ITADVKEAFT GVHYAILVGA MPRREGMERA DLLKANAAIF KVQGKALAEH ANKNVKVLVV GNPANTNALI AQVSANGIPK ENFTCLTRLD QNRAKSQIAL KAGVNVKDVH NVIIWGNHSS TQYPDYRCGY INLSTGKTPI STAIKDEKWL QGEFISTVQK RGAAVIAARK LSSAASAAKA ITDHMHDWVL GTAEGEYVSM GVYSDGSYGV PEGLIFSFPV KCANGKYTIV QGLQMDDLSK NLINLTTEEL VAEKTTALQF LSE //