DMLA_ECOLI
ID DMLA_ECOLI Reviewed; 361 AA.
AC P76251; O08474; O08475;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=D-malate dehydrogenase [decarboxylating];
DE EC=1.1.1.83;
DE AltName: Full=D-malate degradation protein A;
DE AltName: Full=D-malate oxidase;
GN Name=dmlA; Synonyms=yeaU; OrderedLocusNames=b1800, JW1789;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17088549; DOI=10.1073/pnas.0603364103;
RA Reed J.L., Patel T.R., Chen K.H., Joyce A.R., Applebee M.K., Herring C.D.,
RA Bui O.T., Knight E.M., Fong S.S., Palsson B.O.;
RT "Systems approach to refining genome annotation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17480-17484(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ROLE IN D-MALATE
RP UTILIZATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20233924; DOI=10.1128/jb.01665-09;
RA Lukas H., Reimann J., Kim O.B., Grimpo J., Unden G.;
RT "Regulation of aerobic and anaerobic D-malate metabolism of Escherichia
RT coli by the LysR-type regulator DmlR (YeaT).";
RL J. Bacteriol. 192:2503-2511(2010).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidative decarboxylation of
CC D-malate into pyruvate. Is essential for aerobic growth on D-malate as
CC the sole carbon source. But is not required for anaerobic D-malate
CC utilization, although DmlA is expressed and active in those conditions.
CC Appears to be not able to use L-tartrate as a substrate for
CC dehydrogenation instead of D-malate. {ECO:0000269|PubMed:20233924}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC Xref=Rhea:RHEA:18365, ChEBI:CHEBI:15361, ChEBI:CHEBI:15588,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.83;
CC Evidence={ECO:0000269|PubMed:17088549, ECO:0000269|PubMed:20233924};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC P76251; P0CE47: tufA; NbExp=2; IntAct=EBI-560661, EBI-301077;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: By the transcriptional regulator DmlR in the presence of D-
CC malate or L- or meso-tartrate, under aerobic conditions. Is not induced
CC by L-malate, D-tartrate or succinate. Is also induced at high levels
CC under anaerobic conditions in the presence of D-malate and its
CC expression is more than 5-fold greater than the one under aerobic
CC conditions. Repressed by glucose or nitrate under anaerobic conditions.
CC During aerobic growth, appears to be repressed by the DcuS-DcuR two-
CC component system, and is not repressed by glucose.
CC {ECO:0000269|PubMed:20233924}.
CC -!- DISRUPTION PHENOTYPE: Deletion of dmlA inhibits aerobic growth on D-
CC malate but does not impair slow anaerobic growth on D-malate.
CC {ECO:0000269|PubMed:17088549, ECO:0000269|PubMed:20233924}.
CC -!- MISCELLANEOUS: Aerobic growth on D-malate requires, in addition to
CC DmlA, the presence of the aerobic C4-dicarboxylate transporter DctA,
CC for D-malate uptake. Meso-tartrate or L-tartrate are not able to
CC support aerobic growth. Slow anaerobic growth on D-malate is observed
CC only when glycerol is also provided as an electron donor, and D-malate
CC is used in fumarate respiration, so is not dependent on DmlA.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; U00096; AAC74870.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15595.1; -; Genomic_DNA.
DR PIR; H64940; H64940.
DR RefSeq; NP_416314.1; NC_000913.3.
DR RefSeq; WP_000978494.1; NZ_STEB01000009.1.
DR AlphaFoldDB; P76251; -.
DR SMR; P76251; -.
DR BioGRID; 4260335; 22.
DR DIP; DIP-11800N; -.
DR IntAct; P76251; 3.
DR STRING; 511145.b1800; -.
DR jPOST; P76251; -.
DR PaxDb; P76251; -.
DR PRIDE; P76251; -.
DR EnsemblBacteria; AAC74870; AAC74870; b1800.
DR EnsemblBacteria; BAA15595; BAA15595; BAA15595.
DR GeneID; 66674311; -.
DR GeneID; 946319; -.
DR KEGG; ecj:JW1789; -.
DR KEGG; eco:b1800; -.
DR PATRIC; fig|1411691.4.peg.453; -.
DR EchoBASE; EB3280; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_1_6; -.
DR InParanoid; P76251; -.
DR OMA; KLFRQPS; -.
DR PhylomeDB; P76251; -.
DR BioCyc; EcoCyc:G6986-MON; -.
DR BioCyc; MetaCyc:G6986-MON; -.
DR BRENDA; 1.1.1.83; 2026.
DR PRO; PR:P76251; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0046553; F:D-malate dehydrogenase (decarboxylating) activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009027; F:tartrate dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0006108; P:malate metabolic process; IDA:UniProtKB.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR011829; TTC_DH.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR02089; TTC; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..361
FT /note="D-malate dehydrogenase [decarboxylating]"
FT /id="PRO_0000083818"
FT BINDING 224
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P37412"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P37412"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P37412"
SQ SEQUENCE 361 AA; 40315 MW; 6D77B609729925D7 CRC64;
MMKTMRIAAI PGDGIGKEVL PEGIRVLQAA AERWGFALSF EQMEWASCEY YSHHGKMMPD
DWHEQLSRFD AIYFGAVGWP DTVPDHISLW GSLLKFRREF DQYVNLRPVR LFPGVPCPLA
GKQPGDIDFY VVRENTEGEY SSLGGRVNEG TEHEVVIQES VFTRRGVDRI LRYAFELAQS
RPRKTLTSAT KSNGLAISMP YWDERVEAMA ENYPEIRWDK QHIDILCARF VMQPERFDVV
VASNLFGDIL SDLGPACTGT IGIAPSANLN PERTFPSLFE PVHGSAPDIY GKNIANPIAT
IWAGAMMLDF LGNGDERFQQ AHNGILAAIE EVIAHGPKTP DMKGNATTPQ VADAICKIIL
R
