MDH_KLEPN
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-AUG-2022, entry version 59.
DE RecName: Full=Malate dehydrogenase;
DE EC=1.1.1.37;
DE Flags: Fragments;
GN Name=mdh;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; 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,
RC ATCC 13883 / DSM 30104 / JCM 1662 / NBRC 14940 / NCIMB 13281 / NCTC 9633,
RC ES694:2, HU653:4, JO436:1, JO757:2, KK427:2, MA207:1, OR803:4, OR95:2, SB1,
RC SB18, SB30, SB31, SB59, SB95, SB96, SO661:2, UD1001:4, UD580:1, UD711:2,
RC UD827:1, UD890:1, UD892:1, 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}.
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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 InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00056; Ldh_1_N; 1.
DR SUPFAM; SSF51735; SSF51735; 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
