MDH_CHLTE
ID MDH_CHLTE Reviewed; 310 AA.
AC P80039; P94677;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 3.
DT 03-AUG-2022, entry version 164.
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=CT1507;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
RN [3]
RP PROTEIN SEQUENCE OF 1-34.
RX PubMed=1735722; DOI=10.1128/jb.174.4.1307-1313.1992;
RA Charnock C.B., Refseth U.H., Strevaag R.;
RT "Malate dehydrogenase from Chlorobium vibrioforme, Chlorobium tepidum, and
RT Heliobacterium gestii: purification, characterization, and investigation of
RT dinucleotide binding by dehydrogenases by use of empirical methods of
RT protein sequence analysis.";
RL J. Bacteriol. 174:1307-1313(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, 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}.
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; X80838; CAA56810.1; -; Genomic_DNA.
DR EMBL; AE006470; AAM72734.1; -; Genomic_DNA.
DR RefSeq; NP_662392.1; NC_002932.3.
DR RefSeq; WP_010933173.1; NC_002932.3.
DR PDB; 1GUZ; X-ray; 2.00 A; A/B/C/D=1-71.
DR PDB; 1GV0; X-ray; 2.50 A; A/B=1-310.
DR PDBsum; 1GUZ; -.
DR PDBsum; 1GV0; -.
DR AlphaFoldDB; P80039; -.
DR SMR; P80039; -.
DR STRING; 194439.CT1507; -.
DR PRIDE; P80039; -.
DR EnsemblBacteria; AAM72734; AAM72734; CT1507.
DR KEGG; cte:CT1507; -.
DR PATRIC; fig|194439.7.peg.1367; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_10; -.
DR OMA; ASCAEYI; -.
DR OrthoDB; 870724at2; -.
DR EvolutionaryTrace; P80039; -.
DR Proteomes; UP000001007; Chromosome.
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; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..310
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113448"
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 ECO:0000269|PubMed:12054817"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487,
FT ECO:0000269|PubMed:12054817"
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 ECO:0000269|PubMed:12054817"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487,
FT ECO:0000269|PubMed:12054817"
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 CONFLICT 227
FT /note="A -> S (in Ref. 1; CAA56810)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1GV0"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:1GV0"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:1GUZ"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1GUZ"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1GUZ"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1GUZ"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:1GV0"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1GV0"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1GV0"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1GV0"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:1GV0"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1GV0"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1GV0"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:1GV0"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1GV0"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:1GV0"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1GV0"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:1GV0"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:1GV0"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:1GV0"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:1GV0"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1GV0"
FT HELIX 226..240
FT /evidence="ECO:0007829|PDB:1GV0"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:1GV0"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1GV0"
FT STRAND 260..271
FT /evidence="ECO:0007829|PDB:1GV0"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:1GV0"
FT HELIX 285..304
FT /evidence="ECO:0007829|PDB:1GV0"
SQ SEQUENCE 310 AA; 33092 MW; 30A92ACFE9442A93 CRC64;
MKITVIGAGN VGATTAFRLA EKQLARELVL LDVVEGIPQG KALDMYESGP VGLFDTKVTG
SNDYADTANS DIVVITAGLP RKPGMTREDL LSMNAGIVRE VTGRIMEHSK NPIIVVVSNP
LDIMTHVAWQ KSGLPKERVI GMAGVLDSAR FRSFIAMELG VSMQDVTACV LGGHGDAMVP
VVKYTTVAGI PVADLISAER IAELVERTRT GGAEIVNHLK QGSAFYAPAT SVVEMVESIV
LDRKRVLTCA VSLDGQYGID GTFVGVPVKL GKNGVEHIYE IKLDQSDLDL LQKSAKIVDE
NCKMLDASQG
