ID MDHA_DICDI Reviewed; 391 AA. AC Q54GE6; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 24-JAN-2024, entry version 109. DE RecName: Full=Probable malate dehydrogenase 1; DE EC=1.1.1.37; GN Name=mdhA; ORFNames=DDB_G0290207; 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). RN [2] RP PROTEIN SEQUENCE OF 35-45 AND 201-214, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RA Bienvenut W.V., Veltman D.M., Insall R.H.; RL Submitted (JAN-2010) to UniProtKB. 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; AAFI02000161; EAL62325.1; -; Genomic_DNA. DR RefSeq; XP_635832.1; XM_630740.1. DR AlphaFoldDB; Q54GE6; -. DR SMR; Q54GE6; -. DR STRING; 44689.Q54GE6; -. DR PaxDb; 44689-DDB0230186; -. DR EnsemblProtists; EAL62325; EAL62325; DDB_G0290207. DR GeneID; 8627540; -. DR KEGG; ddi:DDB_G0290207; -. DR dictyBase; DDB_G0290207; mdhA. DR eggNOG; KOG1496; Eukaryota. DR HOGENOM; CLU_040727_2_0_1; -. DR InParanoid; Q54GE6; -. DR OMA; TKGMERG; -. DR PhylomeDB; Q54GE6; -. DR Reactome; R-DDI-70263; Gluconeogenesis. DR PRO; PR:Q54GE6; -. DR Proteomes; UP000002195; Chromosome 5. 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:SF3; MALATE DEHYDROGENASE, CYTOPLASMIC; 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 Direct protein sequencing; NAD; Oxidoreductase; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1..391 FT /note="Probable malate dehydrogenase 1" FT /id="PRO_0000312365" FT ACT_SITE 244 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 68..74 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 149 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 155 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 162 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 169 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 186..188 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 188 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 219 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 391 AA; 42265 MW; E9433362AD830967 CRC64; MEQAILRINN ISSQLTGKCP FKAHGGGAGK CPYKLGGGQI LDQSKAWSLV NVTANVDQVT PIKVLVTGAA GQIAYSLMFM IASGQMFGPH QPVILHLLDI PKMADALKGV VMELQDCSYP LLQSVVATTD IQTAFLHINV AILVGAFPRG PGMQRKDLLK VNVSIFKEQG EALNKYASRG VKVLVVGNPA NTNALTALMK ASDLPTSNFS ALTRLDQNRA QSMISEKVGT NVDNVHNVII WGNHSQTQVP DVNHGYILNY PNRGLIEPIP SSVNDDKWLN EQFIPLVQNR GATVIAARKL SSAASAANAI VGHVRDWLLG TKDGEHVSMA VYSDGSYNVP KGLIFSFPVT CHNGQWTIVQ GLKINSSTQQ KIDATIKELQ EEKETAMSFL N //