ID C7NF16_KYTSD Unreviewed; 342 AA. AC C7NF16; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|HAMAP-Rule:MF_01517}; DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|HAMAP-Rule:MF_01517}; GN Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517}; GN OrderedLocusNames=Ksed_07840 {ECO:0000313|EMBL:ACV05840.1}; OS Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541) OS (Micrococcus sedentarius). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae; OC Kytococcus. OX NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV05840.1, ECO:0000313|Proteomes:UP000006666}; RN [1] {ECO:0000313|EMBL:ACV05840.1, ECO:0000313|Proteomes:UP000006666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541 RC {ECO:0000313|Proteomes:UP000006666}; RX PubMed=21304632; DOI=10.4056/sigs.761; RA Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F., RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N., RA Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Schneider S., RA Goker M., Pukall R., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Kytococcus sedentarius type strain (541)."; RL Stand. Genomic Sci. 1:12-20(2009). CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. CC {ECO:0000256|HAMAP-Rule:MF_01517}. 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:0000256|HAMAP-Rule:MF_01517, CC ECO:0000256|RuleBase:RU000422}; CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family. CC {ECO:0000256|ARBA:ARBA00009613, ECO:0000256|HAMAP-Rule:MF_01517}. 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; CP001686; ACV05840.1; -; Genomic_DNA. DR AlphaFoldDB; C7NF16; -. DR STRING; 478801.Ksed_07840; -. DR KEGG; kse:Ksed_07840; -. DR eggNOG; COG0039; Bacteria. DR HOGENOM; CLU_040727_2_0_11; -. DR Proteomes; UP000006666; Chromosome. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule. DR CDD; cd01338; MDH_choloroplast_like; 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; IPR010945; Malate_DH_type2. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01759; MalateDH-SF1; 1. DR PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1. DR PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-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 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|PIRSR:PIRSR000102-3}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517, KW ECO:0000256|RuleBase:RU003369}; KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517, KW ECO:0000256|RuleBase:RU000422}. FT DOMAIN 17..161 FT /note="Lactate/malate dehydrogenase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00056" FT DOMAIN 168..335 FT /note="Lactate/malate dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02866" FT ACT_SITE 199 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-1" FT BINDING 23..29 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 104 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 110 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 117 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 124 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517" FT BINDING 141..143 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517" FT BINDING 143 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 174 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-2" SQ SEQUENCE 342 AA; 36294 MW; 05F90D2930964E83 CRC64; MAQIHVITQE VLVTQPVKVA VTGAAGQIGY SLLFRIASGE LLGPDTPVQL RLLEITPALE ALEGVVMELD DSAFPLLSGV EIGDDANTIF DGANVALLVG ARPRGKGMER SDLLEANGQI FTGQGKALND NAADDIRVTV TGNPANTNAL ITMNNAPDIP AERFSALTRL DHNRALAQLA KKAGVSINDI QRMTIWGNHS ATQYPDIFHA TINGENAAEV VDDQQWLEND FIPTVSQRGA AIIEARGSSS AASAASATID HTRTWLSGTA EGNWTSMAVR SDGSYGVPEG LISSFPVTTK DGEYEIVQGL EINEFSQGKI DATVAELSEE RDTVRAKGLI EG //