MDH_PROVB
ID MDH_PROVB Reviewed; 310 AA.
AC P0C890; P80038; P94687;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
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};
OS Prosthecochloris vibrioformis (Chlorobium vibrioforme).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=1098;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8955383; DOI=10.1128/jb.178.24.7047-7052.1996;
RA Naterstad K., Lauvrak V., Sirevag R.;
RT "Malate dehydrogenase from the mesophile Chlorobium vibrioforme and from
RT the mild thermophile Chlorobium tepidum: molecular cloning, construction of
RT a hybrid, and expression in Escherichia coli.";
RL J. Bacteriol. 178:7047-7052(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND 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).
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; arranged as a dimer of dimers.
CC {ECO:0000269|PubMed:12054817}.
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; X80837; CAA56809.1; -; Genomic_DNA.
DR PDB; 1GUZ; X-ray; 2.00 A; A/B/C/D=72-310.
DR PDB; 1GV1; X-ray; 2.50 A; A/B/C/D=1-310.
DR PDBsum; 1GUZ; -.
DR PDBsum; 1GV1; -.
DR AlphaFoldDB; P0C890; -.
DR SMR; P0C890; -.
DR EvolutionaryTrace; P0C890; -.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
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; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..310
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113449"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:1GUZ"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:1GV1"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1GV1"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1GV1"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1GV1"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1GV1"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1GV1"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1GV1"
FT HELIX 87..108
FT /evidence="ECO:0007829|PDB:1GUZ"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1GUZ"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1GUZ"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1GUZ"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:1GUZ"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:1GUZ"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1GUZ"
FT STRAND 260..271
FT /evidence="ECO:0007829|PDB:1GUZ"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 285..303
FT /evidence="ECO:0007829|PDB:1GUZ"
SQ SEQUENCE 310 AA; 33273 MW; DFF3033B27FEC714 CRC64;
MKITVIGAGN VGATTAFRIA DKKLARELVL LDVVEGIPQG KGLDMYETGP VGLFDTKITG
SNDYADTADS DIVIITAGLP RKPGMTREDL LMKNAGIVKE VTDNIMKHSK NPIIIVVSNP
LDIMTHVAWV RSGLPKERVI GMAGVLDAAR FRSFIAMELG VSMQDINACV LGGHGDAMVP
VVKYTTVAGI PISDLLPAET IDKLVERTRN GGAEIVEHLK QGSAFYSPGS SVVEMVESIV
LDRKRVLPCA VGLEGQYGID KTFVGVPVKL GRNGVEQIYE INLDQADLDL LQKSAKIVDE
NCKMLESTIG
