MDH_STRCO
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 03-AUG-2022, entry version 135.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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=0.150 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.SCO4827; -.
DR GeneID; 1100268; -.
DR KEGG; sco:SCO4827; -.
DR PATRIC; fig|100226.15.peg.4903; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_040727_2_0_11; -.
DR InParanoid; Q9K3J3; -.
DR OMA; TKGMERG; -.
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 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 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
