ID   MDH_LEGPC               Reviewed;         330 AA.
AC   A5IEF4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
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};
GN   OrderedLocusNames=LPC_1821;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000675; ABQ55754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5IEF4; -.
DR   SMR; A5IEF4; -.
DR   KEGG; lpc:LPC_1821; -.
DR   HOGENOM; CLU_040727_2_0_6; -.
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; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..330
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_1000068605"
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"
SQ   SEQUENCE   330 AA;  36019 MW;  A83EFC45BFD2C4D5 CRC64;
     MINNRVRVAV 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
//