MDH_CHLAA
ID MDH_CHLAA Reviewed; 309 AA.
AC P80040; A9WH38;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00487};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00487};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_00487}; OrderedLocusNames=Caur_0900;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8661927; DOI=10.1007/s002030050337;
RA Synstad B., Emmerhoff O., Sirevag R.;
RT "Malate dehydrogenase from the green gliding bacterium Chloroflexus
RT aurantiacus is phylogenetically related to lactic dehydrogenases.";
RL Arch. Microbiol. 165:346-353(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
RN [3]
RP PROTEIN SEQUENCE OF 1-35, AND SUBUNIT.
RX PubMed=3133356; DOI=10.1128/jb.170.7.2947-2953.1988;
RA Rolstad A.K., Howland E., Sirevag R.;
RT "Malate dehydrogenase from the thermophilic green bacterium Chloroflexus
RT aurantiacus: purification, molecular weight, amino acid composition, and
RT partial amino acid sequence.";
RL J. Bacteriol. 170:2947-2953(1988).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 11-306 IN COMPLEX WITH NAD, AND
RP SUBUNIT.
RX PubMed=12054817; DOI=10.1016/s0022-2836(02)00050-5;
RA Dalhus B., Saarinen M., Sauer U.H., Eklund P., Johansson K., Karlsson A.,
RA Ramaswamy S., Bjoerk A., Synstad B., Naterstad K., Sirevaag R., Eklund H.;
RT "Structural basis for thermophilic protein stability: structures of
RT thermophilic and mesophilic malate dehydrogenases.";
RL J. Mol. Biol. 318:707-721(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANT CYS-187 IN COMPLEX WITH
RP NAD AND SUBSTRATE ANALOG, AND SUBUNIT.
RX PubMed=14636605; DOI=10.1016/j.jmb.2003.10.006;
RA Bjoerk A., Dalhus B., Mantzilas D., Eijsink V.G.H., Sirevaag R.;
RT "Stabilization of a tetrameric malate dehydrogenase by introduction of a
RT disulfide bridge at the dimer-dimer interface.";
RL J. Mol. Biol. 334:811-821(2003).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000255|HAMAP-Rule:MF_00487}.
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_00487};
CC -!- SUBUNIT: Homotetramer (active enzyme); homodimer and homotrimer at
CC temperatures lower than 55 degrees Celsius (inactive forms).
CC {ECO:0000269|PubMed:12054817, ECO:0000269|PubMed:14636605,
CC ECO:0000269|PubMed:3133356}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC {ECO:0000255|HAMAP-Rule:MF_00487}.
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DR EMBL; X89038; CAA61436.1; -; Genomic_DNA.
DR EMBL; CP000909; ABY34133.1; -; Genomic_DNA.
DR RefSeq; WP_012256789.1; NC_010175.1.
DR RefSeq; YP_001634522.1; NC_010175.1.
DR PDB; 1GUY; X-ray; 2.20 A; A/C=1-309.
DR PDB; 1UR5; X-ray; 1.75 A; A/C=1-309.
DR PDB; 1UXG; X-ray; 1.90 A; A/B=1-309.
DR PDB; 1UXH; X-ray; 2.10 A; A/B=1-309.
DR PDB; 1UXI; X-ray; 2.10 A; A/B=1-309.
DR PDB; 1UXJ; X-ray; 1.75 A; A/C=1-309.
DR PDB; 1UXK; X-ray; 1.80 A; A/C=1-309.
DR PDB; 4CL3; X-ray; 1.70 A; A/D=1-309.
DR PDBsum; 1GUY; -.
DR PDBsum; 1UR5; -.
DR PDBsum; 1UXG; -.
DR PDBsum; 1UXH; -.
DR PDBsum; 1UXI; -.
DR PDBsum; 1UXJ; -.
DR PDBsum; 1UXK; -.
DR PDBsum; 4CL3; -.
DR AlphaFoldDB; P80040; -.
DR SMR; P80040; -.
DR STRING; 324602.Caur_0900; -.
DR DrugBank; DB01677; Fumaric acid.
DR EnsemblBacteria; ABY34133; ABY34133; Caur_0900.
DR KEGG; cau:Caur_0900; -.
DR PATRIC; fig|324602.8.peg.1031; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_0; -.
DR InParanoid; P80040; -.
DR BRENDA; 1.1.1.37; 1352.
DR EvolutionaryTrace; P80040; -.
DR Proteomes; UP000002008; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR CDD; cd01339; LDH-like_MDH; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_00487; Malate_dehydrog_3; 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; IPR011275; Malate_DH_type3.
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 PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..309
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113447"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P61889, ECO:0000255|HAMAP-
FT Rule:MF_00487"
FT BINDING 9..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487,
FT ECO:0000269|PubMed:12054817, ECO:0000269|PubMed:14636605"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487,
FT ECO:0000269|PubMed:12054817, ECO:0000269|PubMed:14636605"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889, ECO:0000255|HAMAP-
FT Rule:MF_00487"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889, ECO:0000255|HAMAP-
FT Rule:MF_00487"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P61889, ECO:0000255|HAMAP-
FT Rule:MF_00487"
FT BINDING 118..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487,
FT ECO:0000269|PubMed:12054817, ECO:0000269|PubMed:14636605"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889, ECO:0000255|HAMAP-
FT Rule:MF_00487"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889, ECO:0000255|HAMAP-
FT Rule:MF_00487"
FT MUTAGEN 187
FT /note="T->C: Forms an intersubunit disulfide bridge, which
FT makes the enzyme more resistant to thermal denaturation.
FT The mutation does not alter the quaternary structure of the
FT enzyme."
FT CONFLICT 34
FT /note="F -> I (in Ref. 1; CAA61436 and 3)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 90..106
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1UXJ"
FT HELIX 122..133
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 145..160
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:1UXK"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1UXJ"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 246..256
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 261..272
FT /evidence="ECO:0007829|PDB:1UR5"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1UR5"
FT HELIX 286..306
FT /evidence="ECO:0007829|PDB:1UR5"
SQ SEQUENCE 309 AA; 32751 MW; AE1BACC5D5B36331 CRC64;
MRKKISIIGA GFVGSTTAHW LAAKELGDIV LLDFVEGVPQ GKALDLYEAS PIEGFDVRVT
GTNNYADTAN SDVIVVTSGA PRKPGMSRED LIKVNADITR ACISQAAPLS PNAVIIMVNN
PLDAMTYLAA EVSGFPKERV IGQAGVLDAA RYRTFIAMEA GVSVEDVQAM LMGGHGDEMV
PLPRFSTISG IPVSEFIAPD RLAQIVERTR KGGGEIVNLL KTGSAYYAPA AATAQMVEAV
LKDKKRVMPV AAYLTGQYGL NDIYFGVPVI LGAGGVEKIL ELPLNEEEMA LLNASAKAVR
ATLDTLKSL
