MDH_BRUA2
ID MDH_BRUA2 Reviewed; 320 AA.
AC Q2YLR9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=BAB1_1927;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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 -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC {ECO:0000255|HAMAP-Rule:MF_00487}.
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DR EMBL; AM040264; CAJ11883.1; -; Genomic_DNA.
DR RefSeq; WP_002964995.1; NZ_KN046823.1.
DR PDB; 3GVH; X-ray; 2.30 A; A/B/C/D=1-320.
DR PDB; 3GVI; X-ray; 2.25 A; A/B/C/D/E/F=1-320.
DR PDBsum; 3GVH; -.
DR PDBsum; 3GVI; -.
DR AlphaFoldDB; Q2YLR9; -.
DR SMR; Q2YLR9; -.
DR STRING; 359391.BAB1_1927; -.
DR EnsemblBacteria; CAJ11883; CAJ11883; BAB1_1927.
DR GeneID; 3788794; -.
DR KEGG; bmf:BAB1_1927; -.
DR PATRIC; fig|359391.11.peg.1168; -.
DR HOGENOM; CLU_045401_2_1_5; -.
DR OMA; ASCAEYI; -.
DR PhylomeDB; Q2YLR9; -.
DR EvolutionaryTrace; Q2YLR9; -.
DR Proteomes; UP000002719; Chromosome I.
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; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..320
FT /note="Malate dehydrogenase"
FT /id="PRO_0000241943"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 119..121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:3GVI"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3GVI"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 39..54
FT /evidence="ECO:0007829|PDB:3GVI"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:3GVI"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 91..110
FT /evidence="ECO:0007829|PDB:3GVI"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3GVI"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 146..161
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:3GVI"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:3GVI"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 205..216
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:3GVI"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:3GVH"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:3GVI"
FT STRAND 252..262
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3GVI"
FT STRAND 267..278
FT /evidence="ECO:0007829|PDB:3GVI"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 292..315
FT /evidence="ECO:0007829|PDB:3GVI"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3GVI"
SQ SEQUENCE 320 AA; 33704 MW; C212BA88F0241677 CRC64;
MARNKIALIG SGMIGGTLAH LAGLKELGDV VLFDIAEGTP QGKGLDIAES SPVDGFDAKF
TGANDYAAIE GADVVIVTAG VPRKPGMSRD DLLGINLKVM EQVGAGIKKY APEAFVICIT
NPLDAMVWAL QKFSGLPAHK VVGMAGVLDS ARFRYFLSEE FNVSVEDVTV FVLGGHGDSM
VPLARYSTVA GIPLPDLVKM GWTSQDKLDK IIQRTRDGGA EIVGLLKTGS AFYAPAASAI
QMAESYLKDK KRVLPVAAQL SGQYGVKDMY VGVPTVIGAN GVERIIEIDL DKDEKAQFDK
SVASVAGLCE ACIGIAPSLK
