MDH_VIBVU
ID MDH_VIBVU Reviewed; 310 AA.
AC Q8DEC2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01516};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01516};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_01516}; OrderedLocusNames=VV1_0673;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000255|HAMAP-Rule:MF_01516}.
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_01516};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01516}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01516}.
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; AE016795; AAO09185.1; -; Genomic_DNA.
DR RefSeq; WP_011078751.1; NC_004459.3.
DR PDB; 4E0B; X-ray; 2.17 A; A/B/C/D=1-310.
DR PDBsum; 4E0B; -.
DR AlphaFoldDB; Q8DEC2; -.
DR SMR; Q8DEC2; -.
DR EnsemblBacteria; AAO09185; AAO09185; VV1_0673.
DR KEGG; vvu:VV1_0673; -.
DR HOGENOM; CLU_047181_1_0_6; -.
DR OMA; MGWTSQA; -.
DR Proteomes; UP000002275; Chromosome 1.
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 CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_01516; Malate_dehydrog_1; 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; IPR001252; Malate_DH_AS.
DR InterPro; IPR010097; Malate_DH_type1.
DR InterPro; IPR023958; Malate_DH_type1_bac.
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 SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR PROSITE; PS00068; MDH; 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_0000113333"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 7..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4E0B"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:4E0B"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:4E0B"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:4E0B"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:4E0B"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:4E0B"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:4E0B"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4E0B"
FT HELIX 88..108
FT /evidence="ECO:0007829|PDB:4E0B"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:4E0B"
FT HELIX 121..134
FT /evidence="ECO:0007829|PDB:4E0B"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:4E0B"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:4E0B"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:4E0B"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4E0B"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4E0B"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:4E0B"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:4E0B"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:4E0B"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:4E0B"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4E0B"
FT HELIX 225..242
FT /evidence="ECO:0007829|PDB:4E0B"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:4E0B"
FT STRAND 261..270
FT /evidence="ECO:0007829|PDB:4E0B"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:4E0B"
FT HELIX 285..308
FT /evidence="ECO:0007829|PDB:4E0B"
SQ SEQUENCE 310 AA; 32168 MW; A9988AA1FF62927A CRC64;
MKVAVIGAAG GIGQALALLL KNRLPAGSDL ALYDIAPVTP GVAADLSHIP THVSIKGYAG
EDPTPALEGA DVVLISAGVA RKPGMDRADL FNVNAGIVKS LAERIAVVCP NACIGIITNP
VNTTVPIAAE VLKKAGVYDK RKLFGVTTLD VIRSETFVAE LKGQDPGEVR VPVIGGHSGV
TILPLLSQVE GVEFSDEEIA ALTKRIQNAG TEVVEAKAGG GSATLSMGQA ACRFGLALVK
ALQGEEVIEY AYVEGNGEHA SFFAQPVKLG KEGVEEILPY GELSDFEKAA LDGMLETLNS
DIQIGVDFVK
