MDH_MYCBT
ID MDH_MYCBT Reviewed; 329 AA.
AC C1AMN4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517}; OrderedLocusNames=JTY_1275;
OS Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=561275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL Vaccine 27:1710-1716(2009).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000255|HAMAP-Rule:MF_01517}.
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_01517};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01517}.
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DR EMBL; AP010918; BAH25563.1; -; Genomic_DNA.
DR RefSeq; WP_003406301.1; NZ_CP014566.1.
DR AlphaFoldDB; C1AMN4; -.
DR SMR; C1AMN4; -.
DR GeneID; 45425210; -.
DR KEGG; mbt:JTY_1275; -.
DR HOGENOM; CLU_040727_2_0_11; -.
DR OMA; TKGMERG; -.
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 Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_01517; Malate_dehydrog_2; 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; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23382; PTHR23382; 1.
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; TIGR01759; MalateDH-SF1; 1.
DR PROSITE; PS00068; MDH; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..329
FT /note="Malate dehydrogenase"
FT /id="PRO_1000185084"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 12..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 130..132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
SQ SEQUENCE 329 AA; 34322 MW; 0A512659617F9C37 CRC64;
MSASPLKVAV TGAAGQIGYS LLFRLASGSL LGPDRPIELR LLEIEPALQA LEGVVMELDD
CAFPLLSGVE IGSDPQKIFD GVSLALLVGA RPRGAGMERS DLLEANGAIF TAQGKALNAV
AADDVRVGVT GNPANTNALI AMTNAPDIPR ERFSALTRLD HNRAISQLAA KTGAAVTDIK
KMTIWGNHSA TQYPDLFHAE VAGKNAAEVV NDQAWIEDEF IPTVAKRGAA IIDARGASSA
ASAASATIDA ARDWLLGTPA DDWVSMAVVS DGSYGVPEGL ISSFPVTTKG GNWTIVSGLE
IDEFSRGRID KSTAELADER SAVTELGLI
