ID MDH_PECCC Reviewed; 154 AA. AC P61897; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 1. DT 03-MAY-2023, entry version 75. DE RecName: Full=Malate dehydrogenase; DE EC=1.1.1.37; DE Flags: Fragment; GN Name=mdh; OS Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. OS carotovora). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Pectobacterium. OX NCBI_TaxID=555; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=WPP1, WPP10, WPP11, WPP12, WPP13, WPP14, WPP15, WPP17, WPP18, RC WPP19, WPP2, WPP20, WPP21, WPP22, WPP24, WPP25, WPP3, WPP4, WPP5, RC WPP6, WPP7, WPP8, and WPP9; RX PubMed=15128563; DOI=10.1128/aem.70.5.3013-3023.2004; RA Yap M.-N., Barak J.D., Charkowski A.O.; RT "Genomic diversity of Erwinia carotovora subsp. carotovora and its RT correlation with virulence."; RL Appl. Environ. Microbiol. 70:3013-3023(2004). 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 -!- SUBUNIT: Homodimer. {ECO:0000250}. 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; AY428968; AAR11889.1; -; Genomic_DNA. DR EMBL; AY428969; AAR11890.1; -; Genomic_DNA. DR EMBL; AY428970; AAR11891.1; -; Genomic_DNA. DR EMBL; AY428971; AAR11892.1; -; Genomic_DNA. DR EMBL; AY428972; AAR11893.1; -; Genomic_DNA. DR EMBL; AY428973; AAR11894.1; -; Genomic_DNA. DR EMBL; AY428974; AAR11895.1; -; Genomic_DNA. DR EMBL; AY428975; AAR11896.1; -; Genomic_DNA. DR EMBL; AY428976; AAR11897.1; -; Genomic_DNA. DR EMBL; AY428977; AAR11898.1; -; Genomic_DNA. DR EMBL; AY428978; AAR11899.1; -; Genomic_DNA. DR EMBL; AY428979; AAR11900.1; -; Genomic_DNA. DR EMBL; AY428980; AAR11901.1; -; Genomic_DNA. DR EMBL; AY428981; AAR11902.1; -; Genomic_DNA. DR EMBL; AY428982; AAR11903.1; -; Genomic_DNA. DR EMBL; AY428983; AAR11904.1; -; Genomic_DNA. DR EMBL; AY428984; AAR11905.1; -; Genomic_DNA. DR EMBL; AY428985; AAR11906.1; -; Genomic_DNA. DR EMBL; AY428986; AAR11907.1; -; Genomic_DNA. DR EMBL; AY428987; AAR11908.1; -; Genomic_DNA. DR EMBL; AY428988; AAR11909.1; -; Genomic_DNA. DR EMBL; AY428989; AAR11910.1; -; Genomic_DNA. DR EMBL; AY428990; AAR11911.1; -; Genomic_DNA. DR AlphaFoldDB; P61897; -. DR SMR; P61897; -. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. 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; 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; IPR036291; NAD(P)-bd_dom_sf. 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 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..>154 FT /note="Malate dehydrogenase" FT /id="PRO_0000113318" FT ACT_SITE 99 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 3 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 9 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 16 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 39..41 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 41 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 75 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 149 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT VARIANT 15..17 FT /note="VNA -> LPF (in strain: WPP3)" FT VARIANT 23..24 FT /note="LV -> WH (in strain: WPP3)" FT VARIANT 32 FT /note="P -> R (in strain: WPP3)" FT VARIANT 49 FT /note="I -> M (in strain: WPP7)" FT VARIANT 106..107 FT /note="PL -> LC (in strain: WPP25)" FT VARIANT 111 FT /note="V -> D (in strain: WPP25)" FT VARIANT 117 FT /note="S -> N (in strain: WPP3 and WPP8)" FT VARIANT 133..134 FT /note="TE -> AQ (in strain: WPP3)" FT VARIANT 137..140 FT /note="EAKA -> KPKQ (in strain: WPP19)" FT VARIANT 137 FT /note="E -> K (in strain: WPP3)" FT VARIANT 141 FT /note="G -> R (in strain: WPP25)" FT VARIANT 142 FT /note="G -> A (in strain: WPP9 and WPP10)" FT VARIANT 150..154 FT /note="GQVPG -> ARLPA (in strain: WPP25)" FT VARIANT 152..154 FT /note="VPG -> AAR (in strain: WPP20, WPP22 and WPP7)" FT VARIANT 152..154 FT /note="VPG -> AGR (in strain: WPP5)" FT VARIANT 152..153 FT /note="VP -> AA (in strain: WPP12 and WPP21)" FT VARIANT 152 FT /note="V -> A (in strain: WPP24)" FT VARIANT 153 FT /note="P -> A (in strain: WPP4)" FT NON_TER 1 FT NON_TER 154 SQ SEQUENCE 154 AA; 16149 MW; 40417ECADE8C1877 CRC64; LRRKPGMDRS DLFNVNAGIV RNLVEQIAVT CPKACIGIIT NPVNTTVAIA AEVLKKAGVY DKNKLFGVTT LDIIRSNTFV AELKGKQPQD INVPVIGGHS GVTILPLLSQ VPGISFSEQE VADLTKRIQN AGTEVVEAKA GGGSATLSMG QVPG //