MDH_RAOTE
ID MDH_RAOTE Reviewed; 225 AA.
AC P61895;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Malate dehydrogenase;
DE EC=1.1.1.37;
DE Flags: Fragment;
GN Name=mdh;
OS Raoultella terrigena (Klebsiella terrigena).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Raoultella.
OX NCBI_TaxID=577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33257 / DSM 2687 / JCM 1687 / NBRC 14941 / NCTC 13038 /
RC VTT-E-97854;
RX PubMed=15053318; DOI=10.1078/0723-2020-00261;
RA Rosenblueth M., Martinez L., Silva J., Martinez-Romero E.;
RT "Klebsiella variicola, a novel species with clinical and plant-associated
RT isolates.";
RL Syst. Appl. Microbiol. 27:27-35(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; AY367381; AAQ72407.1; -; Genomic_DNA.
DR AlphaFoldDB; P61895; -.
DR SMR; P61895; -.
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; -; 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; IPR010097; Malate_DH_type1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR PROSITE; PS00068; MDH; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN <1..>225
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113311"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 1
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 61
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 84..86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 225
SQ SEQUENCE 225 AA; 23055 MW; 6E76E81267F09DD0 CRC64;
DIAPVTPGVA VDLSHIPTDV KIKGFSGEDA TPALEGADVV LISAGVARKP GMDRSDLFNV
NAGIVKNLVQ QIAKTSPQAC IGIITNPVNT TVAIAAEVLK KAGVYDKNKL FGVTTLDIIR
SNTFVAELKG KSSSDVEVPV IGGHSGVTIL PLLSQIAGVS FSEQEVADLT KRIQNAGTEV
VEAKAGGGSA TLSMGQAAAR FGLSLVRAMQ GEKGVVECAY VEGDG
