ID MDH_LEGPH Reviewed; 330 AA. AC Q5ZT13; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517}; DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517}; GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517}; OrderedLocusNames=lpg2352; OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC OS 33152 / DSM 7513). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=272624; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513; RX PubMed=15448271; DOI=10.1126/science.1099776; RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V., RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A., RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A., RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A., RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A., RA Russo J.J.; RT "The genomic sequence of the accidental pathogen Legionella pneumophila."; RL Science 305:1966-1968(2004). CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01517}; CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family. CC {ECO:0000255|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; AE017354; AAU28414.1; -; Genomic_DNA. DR RefSeq; WP_010948058.1; NC_002942.5. DR RefSeq; YP_096361.1; NC_002942.5. DR PDB; 6PBL; X-ray; 1.85 A; A/B=1-330. DR PDBsum; 6PBL; -. DR AlphaFoldDB; Q5ZT13; -. DR SMR; Q5ZT13; -. DR STRING; 272624.lpg2352; -. DR PaxDb; 272624-lpg2352; -. DR GeneID; 66491480; -. DR KEGG; lpn:lpg2352; -. DR PATRIC; fig|272624.6.peg.2473; -. DR eggNOG; COG0039; Bacteria. DR HOGENOM; CLU_040727_2_0_6; -. DR OrthoDB; 9802969at2; -. DR Proteomes; UP000000609; 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 1: Evidence at protein level; KW 3D-structure; NAD; Oxidoreductase; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1..330 FT /note="Malate dehydrogenase" FT /id="PRO_0000113372" FT ACT_SITE 188 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 12..18 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 93 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 106 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 113 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 130..132 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 132 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 163 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT STRAND 5..10 FT /evidence="ECO:0007829|PDB:6PBL" FT TURN 11..14 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 16..26 FT /evidence="ECO:0007829|PDB:6PBL" FT TURN 27..31 FT /evidence="ECO:0007829|PDB:6PBL" FT STRAND 36..42 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 48..59 FT /evidence="ECO:0007829|PDB:6PBL" FT TURN 60..62 FT /evidence="ECO:0007829|PDB:6PBL" FT STRAND 66..73 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 75..79 FT /evidence="ECO:0007829|PDB:6PBL" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 99..120 FT /evidence="ECO:0007829|PDB:6PBL" FT STRAND 126..129 FT /evidence="ECO:0007829|PDB:6PBL" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 134..143 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:6PBL" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 158..171 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:6PBL" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:6PBL" FT TURN 196..198 FT /evidence="ECO:0007829|PDB:6PBL" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 206..210 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 213..218 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 220..225 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 227..235 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 240..255 FT /evidence="ECO:0007829|PDB:6PBL" FT STRAND 264..269 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 273..275 FT /evidence="ECO:0007829|PDB:6PBL" FT STRAND 281..289 FT /evidence="ECO:0007829|PDB:6PBL" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:6PBL" FT HELIX 303..325 FT /evidence="ECO:0007829|PDB:6PBL" SQ SEQUENCE 330 AA; 36007 MW; 3C36348E4E1BCAEA CRC64; MTNNRVRVAV TGAAGQIGYA LVFRIASGQM FGPNTEVELN LLELEPALPS LEGVAMELDD CAFPLLKRIV CTADLNKAMD GVNWALLVGS VPRKQGMERS DLLQINGGIF TKQGQAINDY ASDDVRVFVV GNPCNTNCLI AMNHAKDVPS DRFYAMTTLD ELRARTQLAK KAGVDITAVT QMTIWGNHSA TQYPDFYNAK INGTSAAQVI NDETWLKETF VSTVQQRGAA VIKARGSSSA ASAANAIITG VNHLVTDTPA GESFSMCRRS KGEYGVDEGL IFSFPCRREH GELKVVENLE FNDFGRERFN TTLNELRSER DTVKSLGLLD //