ID MDH_KLEPN Reviewed; 135 AA. AC P0C1G4; P80535; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 1. DT 03-MAY-2023, entry version 62. DE RecName: Full=Malate dehydrogenase; DE EC=1.1.1.37; DE Flags: Fragments; GN Name=mdh; OS Klebsiella pneumoniae. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=573; RN [1] RP PROTEIN SEQUENCE OF 1-21. RX PubMed=9190829; DOI=10.1128/jb.179.12.4066-4070.1997; RA Charnock C.; RT "Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas RT species are the first reported MDHs in Proteobacteria which resemble RT lactate dehydrogenases in primary structure."; RL J. Bacteriol. 179:4066-4070(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-135. RC STRAIN=1976E, ATCC 11296, ATCC 13883 / DSM 30104 / JCM 1662 / NBRC RC 14940 / NCIMB 13281 / NCTC 9633, ES694:2, HU653:4, JO436:1, JO757:2, RC KK427:2, MA207:1, OR803:4, OR95:2, SB1, SB18, SB30, SB31, SB59, SB95, RC SB96, SO661:2, UD1001:4, UD580:1, UD711:2, UD827:1, UD890:1, UD892:1, RC and VA680:2; RX PubMed=15215087; DOI=10.1128/aac.48.7.2400-2408.2004; RA Haeggman S., Loefdahl S., Paauw A., Verhoef J., Brisse S.; RT "Diversity and evolution of the class A chromosomal beta-lactamase gene in RT Klebsiella pneumoniae."; RL Antimicrob. Agents Chemother. 48:2400-2408(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; AJ635372; CAG25783.1; -; Genomic_DNA. DR EMBL; AJ635373; CAG25784.1; -; Genomic_DNA. DR EMBL; AJ635374; CAG25785.1; -; Genomic_DNA. DR EMBL; AJ635375; CAG25786.1; -; Genomic_DNA. DR EMBL; AJ635376; CAG25787.1; -; Genomic_DNA. DR EMBL; AJ635377; CAG25788.1; -; Genomic_DNA. DR EMBL; AJ635378; CAG25789.1; -; Genomic_DNA. DR EMBL; AJ635380; CAG25791.1; -; Genomic_DNA. DR EMBL; AJ635381; CAG25792.1; -; Genomic_DNA. DR EMBL; AJ635382; CAG25793.1; -; Genomic_DNA. DR EMBL; AJ635383; CAG25794.1; -; Genomic_DNA. DR EMBL; AJ635384; CAG25795.1; -; Genomic_DNA. DR EMBL; AJ635385; CAG25796.1; -; Genomic_DNA. DR EMBL; AJ635386; CAG25797.1; -; Genomic_DNA. DR EMBL; AJ635387; CAG25798.1; -; Genomic_DNA. DR EMBL; AJ635388; CAG25799.1; -; Genomic_DNA. DR EMBL; AJ635389; CAG25800.1; -; Genomic_DNA. DR EMBL; AJ635390; CAG25801.1; -; Genomic_DNA. DR EMBL; AJ635392; CAG25803.1; -; Genomic_DNA. DR EMBL; AJ635393; CAG25804.1; -; Genomic_DNA. DR EMBL; AJ635394; CAG25805.1; -; Genomic_DNA. DR EMBL; AJ635395; CAG25806.1; -; Genomic_DNA. DR EMBL; AJ635396; CAG25807.1; -; Genomic_DNA. DR EMBL; AJ635397; CAG25808.1; -; Genomic_DNA. DR EMBL; AJ635398; CAG25809.1; -; Genomic_DNA. DR EMBL; AJ635399; CAG25810.1; -; Genomic_DNA. 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; IPR001236; Lactate/malate_DH_N. 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; PF00056; Ldh_1_N; 1. 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..>135 FT /note="Malate dehydrogenase" FT /id="PRO_0000113310" FT BINDING 7..12 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 25 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 72 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 78 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 85 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 108..110 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 110 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT VARIANT 63 FT /note="V -> I (in strain: ES694:2)" FT VARIANT 99 FT /note="T -> N (in strain: UD711:2 and VA680:2)" FT VARIANT 107 FT /note="I -> V (in strain: SB1, SB31, SB95, SB96, SO661:2, FT OR803:4, UD711:2, JO757:2, JO436:1, KK427:2, UD827:1, FT UD892:1 and VA680:2)" FT VARIANT 127 FT /note="G -> D (in strain: ES694:2)" FT NON_CONS 21..22 FT /evidence="ECO:0000305" FT NON_TER 135 SQ SEQUENCE 135 AA; 13935 MW; E8379B36BB9BD94B CRC64; MKVAVLXAAG GIQALALLLK TSLYDIAPVT PGVAVDLSHI PTDVKIKGFS GEDATPALEG ADVVLISAGV ARKPGMDRSD LFNVNAGIVK NLVQQIAKTC PQACIGIITN PVNTTVAIAA EVLKKAGVYD KNKLF //