ID   MDH_STRCO               Reviewed;         329 AA.
AC   Q9K3J3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000303|PubMed:21071865};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:21071865};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517}; OrderedLocusNames=SCO4827;
GN   ORFNames=SC2A6.12;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=21071865; DOI=10.1271/bbb.100357;
RA   Ge Y.D., Cao Z.Y., Wang Z.D., Chen L.L., Zhu Y.M., Zhu G.P.;
RT   "Identification and biochemical characterization of a thermostable malate
RT   dehydrogenase from the mesophile Streptomyces coelicolor A3(2).";
RL   Biosci. Biotechnol. Biochem. 74:2194-2201(2010).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       Exhibits remarkably higher catalytic efficiency for oxaloacetate
CC       reduction than for malate oxidation in vitro. Shows a high specificity
CC       for NAD(H), being almost inactive with NADP(H).
CC       {ECO:0000269|PubMed:21071865}.
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         ECO:0000269|PubMed:21071865};
CC   -!- ACTIVITY REGULATION: Activity is inhibited by Zn(2+) and Co(2+). No
CC       activity in the presence of Fe(2+). {ECO:0000269|PubMed:21071865}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.189 mM for oxaloacetate {ECO:0000269|PubMed:21071865};
CC         KM=0.083 mM for NADH {ECO:0000269|PubMed:21071865};
CC         KM=0.494 mM for L-malate {ECO:0000269|PubMed:21071865};
CC         KM=0.15 mM for NAD(+) {ECO:0000269|PubMed:21071865};
CC         Vmax=1600 umol/min/mg enzyme toward oxaloacetate
CC         {ECO:0000269|PubMed:21071865};
CC         Vmax=464 umol/min/mg enzyme toward NADH
CC         {ECO:0000269|PubMed:21071865};
CC         Vmax=4.02 umol/min/mg enzyme toward L-malate
CC         {ECO:0000269|PubMed:21071865};
CC         Vmax=3.14 umol/min/mg enzyme toward NAD(+)
CC         {ECO:0000269|PubMed:21071865};
CC         Note=kcat is 1870 sec(-1) with oxaloacetate as substrate. kcat is 542
CC         sec(-1) with NADH as substrate. kcat is 4.71 sec(-1) with L-malate as
CC         substrate. kcat is 3.66 sec(-1) with NAD(+) as substrate.
CC         {ECO:0000269|PubMed:21071865};
CC       pH dependence:
CC         Optimum pH is 6.8 at 50 degrees Celsius and 8.5 at 30 degrees
CC         Celsius. {ECO:0000269|PubMed:21071865};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:21071865};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21071865}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000305}.
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DR   EMBL; AL939121; CAB97430.1; -; Genomic_DNA.
DR   RefSeq; NP_628983.1; NC_003888.3.
DR   RefSeq; WP_003974145.1; NZ_VNID01000016.1.
DR   AlphaFoldDB; Q9K3J3; -.
DR   SMR; Q9K3J3; -.
DR   STRING; 100226.gene:17762476; -.
DR   PaxDb; 100226-SCO4827; -.
DR   PATRIC; fig|100226.15.peg.4903; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_040727_2_0_11; -.
DR   InParanoid; Q9K3J3; -.
DR   OrthoDB; 9802969at2; -.
DR   PhylomeDB; Q9K3J3; -.
DR   BRENDA; 1.1.1.37; 5998.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR   GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   CDD; cd01338; MDH_choloroplast_like; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..329
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113394"
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;  34643 MW;  76E5F74769CCCAF4 CRC64;
     MTRTPVNVTV TGAAGQIGYA LLFRIASGQL LGADVPVKLR LLEITPALKA AEGTAMELDD
     CAFPLLQGIE ITDDPNVAFD GANVALLVGA RPRTKGMERG DLLEANGGIF KPQGKAINDH
     AADDIKVLVV GNPANTNALI AQAAAPDVPA ERFTAMTRLD HNRALTQLAK KTGSTVADIK
     RLTIWGNHSA TQYPDIFHAT VAGKNAAETV NDEKWLADEF IPTVAKRGAA IIEARGASSA
     ASAANAAIDH VYTWVNGTAE GDWTSMGIPS DGSYGVPEGI ISSFPVTTKD GSYEIVQGLD
     INEFSRARID ASVKELSEER EAVRGLGLI
//