MDH_HAEI8
ID MDH_HAEI8 Reviewed; 311 AA.
AC Q4QL89;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=NTHI1381;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX88208.1; -; Genomic_DNA.
DR RefSeq; WP_005657108.1; NC_007146.2.
DR AlphaFoldDB; Q4QL89; -.
DR SMR; Q4QL89; -.
DR PRIDE; Q4QL89; -.
DR EnsemblBacteria; AAX88208; AAX88208; NTHI1381.
DR KEGG; hit:NTHI1381; -.
DR HOGENOM; CLU_047181_0_1_6; -.
DR OMA; MGWTSQA; -.
DR OrthoDB; 870724at2; -.
DR Proteomes; UP000002525; 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 3: Inferred from homology;
KW NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..311
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113307"
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 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
SQ SEQUENCE 311 AA; 32497 MW; 63F64FF9E67FCF3E CRC64;
MKVAVLGAAG GIGQALALLL KLQLPAGTDL ALYDIAPVTP GVAVDVSHIP TAVNVKGFSG
EDPTPALEGA DVVLISAGVA RKPGMDRSDL FNINAGIVRG LIEKVAITCP KACVGIITNP
VNTTVAIAAE VLKKAGVYDK RKLFGVTTLD VLRSETFVAE LKGLNVSRTS VPVIGGHSGV
TILPLLSQVQ YAKWNEDEIE PLAKRIQNAG TEVVNAKAGG GSATLSMAQA AARFARSLVK
GLSGETVVEC TYVEGDGKYA RFFSQPVRLG KEGVEEILPI GPLSNFEQQA LENMLPTLRA
DIELGEKFIN G
