ID MDHM_MACFA Reviewed; 338 AA. AC Q4R568; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 24-JAN-2024, entry version 97. DE RecName: Full=Malate dehydrogenase, mitochondrial; DE EC=1.1.1.37; DE Flags: Precursor; GN Name=MDH2; ORFNames=QccE-17106; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG International consortium for macaque cDNA sequencing and analysis; RT "DNA sequences of macaque genes expressed in brain or testis and its RT evolutionary implications."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. 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 -!- ACTIVITY REGULATION: Enzyme activity is enhanced by acetylation. CC {ECO:0000250|UniProtKB:P40926}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00346}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000250|UniProtKB:P04636}. CC -!- PTM: Acetylation is enhanced after treatment either with trichostin A CC (TCA) or with nicotinamide (NAM) with the appearance of tri- and CC tetraacetylations. Glucose also increases acetylation. CC {ECO:0000250|UniProtKB:P40926}. 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; AB169676; BAE01757.1; -; mRNA. DR RefSeq; NP_001270089.1; NM_001283160.1. DR AlphaFoldDB; Q4R568; -. DR SMR; Q4R568; -. DR STRING; 9541.ENSMFAP00000011294; -. DR GlyCosmos; Q4R568; 1 site, No reported glycans. DR eggNOG; KOG1494; Eukaryota. DR OrthoDB; 5059897at2759; -. DR Proteomes; UP000233100; Unplaced. DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB. DR GO; GO:0030060; F:L-malate dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0009060; P:aerobic respiration; ISS:UniProtKB. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. 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 2: Evidence at transcript level; KW Acetylation; Glycoprotein; Mitochondrion; NAD; Oxidoreductase; KW Phosphoprotein; Reference proteome; Transit peptide; KW Tricarboxylic acid cycle. FT TRANSIT 1..24 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:P00346" FT CHAIN 25..338 FT /note="Malate dehydrogenase, mitochondrial" FT /id="PRO_0000285846" FT ACT_SITE 200 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P00346" FT BINDING 31..37 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 57 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 104 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 110 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 117 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 140..142 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 142 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 176 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 251 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT MOD_RES 78 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 78 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 91 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 91 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 165 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P40926" FT MOD_RES 185 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q32LG3" FT MOD_RES 185 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 203 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 215 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 215 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 239 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 239 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q32LG3" FT MOD_RES 239 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q32LG3" FT MOD_RES 246 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P40926" FT MOD_RES 269 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 296 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 296 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 301 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P40926" FT MOD_RES 301 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q32LG3" FT MOD_RES 314 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q32LG3" FT MOD_RES 314 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 324 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 324 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT MOD_RES 326 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P40926" FT MOD_RES 328 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q32LG3" FT MOD_RES 328 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q32LG3" FT MOD_RES 329 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P40926" FT MOD_RES 329 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q32LG3" FT MOD_RES 335 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P40926" FT MOD_RES 335 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08249" FT CARBOHYD 33 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250|UniProtKB:P04636" SQ SEQUENCE 338 AA; 35565 MW; E2C104CDFD3F468F CRC64; MLSALARPAS AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH TPGVAADLSH IETKAVVKGY LGPEQLPDCL KGCDVVVIPA GVPRKPGMTR DDLFNTNATI VATLAAACAQ HRPEAMICII ANPVNSTIPI TAEVFKKHGV YNPSKIFGVT TLDIVRANTF VAELKGLDPA RVNVPVIGGH AGKTIIPLIS QCTPKVDFPQ DQLTALTGRI QEAGTEVVKA KAGAGSATLS MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETECTYFST PLLLGKKGIE KNLGIGQIPS FEEKMISDAI PELKASIKKG EDFVKTLK //