MDH_CORGL
ID MDH_CORGL Reviewed; 328 AA.
AC Q8NN33; Q8VNW2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16233457};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517};
GN OrderedLocusNames=Cgl2380, cg2613;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RA Kos P.B., Puskas L.G., Hackler L., Yukawa H.;
RT "Cloning, sequencing and expression of the gene encoding malate
RT dehydrogenase in the amino-acid producer Corynebacterium glutamicum.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP PROTEIN SEQUENCE OF 2-9, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 14067 / DSM 20411 / NCIB 9565 / 2247;
RX PubMed=16233457; DOI=10.1263/jbb.95.562;
RA Genda T., Nakamatsu T., Ozak H.;
RT "Purification and characterization of malate dehydrogenase from
RT Corynebacterium glutamicum.";
RL J. Biosci. Bioeng. 95:562-566(2003).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC Exhibits higher catalytic efficiency for oxaloacetate reduction than
CC for malate oxidation in vitro. Almost equally active both for NADH and
CC NADPH on the bases of the kcat values at pH 6.5, but catalytic
CC efficiency for oxaloacetate reduction is 50-fold higher with NADH.
CC {ECO:0000269|PubMed:16233457}.
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:16233457};
CC -!- ACTIVITY REGULATION: Citrate activates the enzyme in the oxidation of
CC malate to oxaloacetate and inhibits it in the reverse reaction.
CC {ECO:0000269|PubMed:16233457}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.025 mM for oxaloacetate (at pH 6.5 in the presence of NADH)
CC {ECO:0000269|PubMed:16233457};
CC KM=0.55 mM for oxaloacetate (at pH 6.5 in the presence of NADPH)
CC {ECO:0000269|PubMed:16233457};
CC KM=0.07 mM for NADH (at pH 6.5) {ECO:0000269|PubMed:16233457};
CC KM=0.25 mM for NADPH (at pH 6.5) {ECO:0000269|PubMed:16233457};
CC KM=0.8 mM for malate (at pH 10.5 in the presence of NAD)
CC {ECO:0000269|PubMed:16233457};
CC KM=0.4 mM for NAD (at pH 10.5) {ECO:0000269|PubMed:16233457};
CC Note=kcat is 360 sec(-1) for NADH-dependent reduction of
CC oxaloacetate. kcat is 150 sec(-1) for NADPH-dependent reduction of
CC oxaloacetate. kcat is 140 sec(-1) for NAD(+)-dependent oxidation of
CC malate. {ECO:0000269|PubMed:16233457};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16233457}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01517}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ303072; CAC83073.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99773.1; -; Genomic_DNA.
DR EMBL; BX927155; CAF21045.1; -; Genomic_DNA.
DR RefSeq; NP_601581.1; NC_003450.3.
DR RefSeq; WP_011015079.1; NC_006958.1.
DR PDB; 6ITK; X-ray; 2.00 A; A/B=1-328.
DR PDBsum; 6ITK; -.
DR AlphaFoldDB; Q8NN33; -.
DR SMR; Q8NN33; -.
DR STRING; 196627.cg2613; -.
DR World-2DPAGE; 0001:Q8NN33; -.
DR KEGG; cgb:cg2613; -.
DR KEGG; cgl:Cgl2380; -.
DR PATRIC; fig|196627.13.peg.2315; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_040727_2_0_11; -.
DR OMA; TKGMERG; -.
DR BRENDA; 1.1.1.37; 960.
DR SABIO-RK; Q8NN33; -.
DR Proteomes; UP000000582; 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 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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16233457"
FT CHAIN 2..328
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113364"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 16..22
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 110
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 134..136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT CONFLICT 274
FT /note="A -> G (in Ref. 1; CAC83073)"
FT /evidence="ECO:0000305"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:6ITK"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:6ITK"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 103..124
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 162..176
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 244..259
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:6ITK"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 304..323
FT /evidence="ECO:0007829|PDB:6ITK"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:6ITK"
SQ SEQUENCE 328 AA; 34908 MW; 1B725310F07A7EB0 CRC64;
MNSPQNVSTK KVTVTGAAGQ ISYSLLWRIA NGEVFGTDTP VELKLLEIPQ ALGGAEGVAM
ELLDSAFPLL RNITITADAN EAFDGANAAF LVGAKPRGKG EERADLLANN GKIFGPQGKA
INDNAADDIR VLVVGNPANT NALIASAAAP DVPASRFNAM MRLDHNRAIS QLATKLGRGS
AEFNNIVVWG NHSATQFPDI TYATVGGEKV TDLVDHDWYV EEFIPRVANR GAEIIEVRGK
SSAASAASSA IDHMRDWVQG TEAWSSAAIP STGAYGIPEG IFVGLPTVSR NGEWEIVEGL
EISDFQRARI DANAQELQAE REAVRDLL
