MDH_SHEON
ID MDH_SHEON Reviewed; 311 AA.
AC P82177;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Malate dehydrogenase;
DE EC=1.1.1.37;
GN Name=mdh; OrderedLocusNames=SO_0770;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2]
RP PROTEIN SEQUENCE OF 3-21.
RC STRAIN=MR-1;
RX PubMed=11135424;
RX DOI=10.1002/1097-0231(20010115)15:1<50::aid-rcm191>3.0.co;2-v;
RA Devreese B., Vanrobaeys F., Van Beeumen J.;
RT "Automated nanoflow liquid chromatography/tandem mass spectrometric
RT identification of proteins from Shewanella putrefaciens separated by two-
RT dimensional polyacrylamide gel electrophoresis.";
RL Rapid Commun. Mass Spectrom. 15:50-56(2001).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000305}.
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DR EMBL; AE014299; AAN53846.1; -; Genomic_DNA.
DR RefSeq; NP_716401.1; NC_004347.2.
DR RefSeq; WP_011071073.1; NZ_CP053946.1.
DR AlphaFoldDB; P82177; -.
DR SMR; P82177; -.
DR STRING; 211586.SO_0770; -.
DR PaxDb; P82177; -.
DR KEGG; son:SO_0770; -.
DR PATRIC; fig|211586.12.peg.740; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_047181_1_0_6; -.
DR OMA; MGWTSQA; -.
DR OrthoDB; 870724at2; -.
DR PhylomeDB; P82177; -.
DR BioCyc; SONE211586:G1GMP-721-MON; -.
DR Proteomes; UP000008186; 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: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 Direct protein sequencing; NAD; Oxidoreductase; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..311
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113326"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 7..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 13
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="L -> LG (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 32137 MW; 9D3F5E86A2500A1B CRC64;
MKVAVLGAAG GIGQALALLL KTQLPAGSKL SLYDIAPVTP GVAVDLSHIP TAVEIKGFAG
EDPTPALVGA DVVLISAGVA RKPGMDRSDL FNINAGIVRN LIEKVAVTCP KALVGIITNP
VNTTVAIAAE VMKKAGVYDK NRLFGVTTLD VIRSETFIAE LKGLNVADVK INVIGGHSGV
TILPLLSQVE GVTFSDEEVA SLTKRIQNAG TEVVEAKAGG GSATLSMGQA ACRFGMSLVR
GLQGEANVVE CAYVDGGSEH AEFFAQPVLL GKNGIEKVLP YGEVSAFEAN ARDSMLDTLK
GDIKLGVDFV K
