MDH_MANSM
ID MDH_MANSM Reviewed; 312 AA.
AC Q65T37;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01516};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01516};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_01516}; OrderedLocusNames=MS1266;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000255|HAMAP-Rule:MF_01516}.
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_01516};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01516}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01516}.
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DR EMBL; AE016827; AAU37873.1; -; Genomic_DNA.
DR RefSeq; WP_011200440.1; NC_006300.1.
DR PDB; 6ITL; X-ray; 1.97 A; A=1-312.
DR PDBsum; 6ITL; -.
DR AlphaFoldDB; Q65T37; -.
DR SMR; Q65T37; -.
DR STRING; 221988.MS1266; -.
DR EnsemblBacteria; AAU37873; AAU37873; MS1266.
DR KEGG; msu:MS1266; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_047181_0_1_6; -.
DR OMA; MGWTSQA; -.
DR OrthoDB; 870724at2; -.
DR Proteomes; UP000000607; Chromosome.
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; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_01516; Malate_dehydrog_1; 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; IPR010097; Malate_DH_type1.
DR InterPro; IPR023958; Malate_DH_type1_bac.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR PROSITE; PS00068; MDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..312
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113313"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 7..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6ITL"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:6ITL"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:6ITL"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:6ITL"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:6ITL"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:6ITL"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:6ITL"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:6ITL"
FT HELIX 87..108
FT /evidence="ECO:0007829|PDB:6ITL"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:6ITL"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6ITL"
FT HELIX 121..134
FT /evidence="ECO:0007829|PDB:6ITL"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:6ITL"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6ITL"
FT HELIX 148..162
FT /evidence="ECO:0007829|PDB:6ITL"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6ITL"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:6ITL"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:6ITL"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6ITL"
FT HELIX 197..218
FT /evidence="ECO:0007829|PDB:6ITL"
FT HELIX 226..243
FT /evidence="ECO:0007829|PDB:6ITL"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:6ITL"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:6ITL"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:6ITL"
FT HELIX 286..311
FT /evidence="ECO:0007829|PDB:6ITL"
SQ SEQUENCE 312 AA; 32423 MW; 1B7466D083335548 CRC64;
MKVAVLGAAG GIGQALALLL KLQLPAGSSL SLYDVAPVTP GVAKDLSHIP TDVVVEGFAG
TDPSEALKGA DIVLISAGVA RKPGMTRADL FGVNAGIIRS LTEKVAEQCP KACVGIITNP
VNAMVAIAAE VLKKAGVYDK RKLFGITTLD ILRAETFIAE LKGLDPTRVT IPVIGGHSGV
TILPLLSQVQ NVEWSSEEEI IALTHRIQNA GTEVVEAKAG GGSATLSMAQ AAARFALALV
KASQGAKVVE CAYVEGDGKY ARFFAQPVRL GTEGVEEYLT LGKLSAFEEK ALNAMLETLQ
GDIKSGEDFI NG
