ID MDH_STRAR Reviewed; 31 AA. AC P19982; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 28-JUN-2023, entry version 83. DE RecName: Full=Malate dehydrogenase; DE EC=1.1.1.37; DE Flags: Fragment; GN Name=mdh; OS Streptomyces atratus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1893; RN [1] RP PROTEIN SEQUENCE. RX PubMed=2775496; DOI=10.1515/bchm3.1989.370.2.763; RA Rommel T.O., Hund H.-K., Speth A.R., Lingens F.; RT "Purification and N-terminal amino-acid sequences of bacterial malate RT dehydrogenases from six actinomycetales strains and from Phenylobacterium RT immobile, strain E."; RL Biol. Chem. Hoppe-Seyler 370:763-768(1989). 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 Evidence={ECO:0000255|PROSITE-ProRule:PRU10004}; 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 PIR; S04960; S04960. DR AlphaFoldDB; P19982; -. DR SMR; P19982; -. DR STRING; 1893.SAMN02787144_1011139; -. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; NAD; Oxidoreductase; Tricarboxylic acid cycle. FT CHAIN 1..>31 FT /note="Malate dehydrogenase" FT /id="PRO_0000113392" FT BINDING 11..17 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT NON_TER 31 SQ SEQUENCE 31 AA; 3155 MW; 2973FDBDA2ACCE3A CRC64; TRTPVNVTVT GAAGQIGYAL LFRIASGHLL G //