ID   DML_EUBBA               Reviewed;         289 AA.
AC   Q0QLE4;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=2,3-dimethylmalate lyase {ECO:0000312|EMBL:ABC88406.1};
DE            EC=4.1.3.32;
GN   Name=Dml {ECO:0000312|EMBL:ABC88406.1};
OS   Eubacterium barkeri (Clostridium barkeri).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1528;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABC88406.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, COFACTOR, AND SUBUNIT.
RC   STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC   5359 {ECO:0000312|EMBL:ABC88406.1};
RX   PubMed=16894175; DOI=10.1073/pnas.0601635103;
RA   Alhapel A., Darley D.J., Wagener N., Eckel E., Elsner N., Pierik A.J.;
RT   "Molecular and functional analysis of nicotinate catabolism in Eubacterium
RT   barkeri.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:12341-12346(2006).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC   5359 {ECO:0000269|PubMed:527937};
RX   PubMed=527937; DOI=10.1515/bchm2.1979.360.2.1693;
RA   Pirzer P., Lill U., Eggerer H.;
RT   "Nicotinic acid metabolism. 2,3-Dimethylmalate lyase.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 360:1693-1702(1979).
RN   [3] {ECO:0000305}
RP   CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC   5359 {ECO:0000269|PubMed:7399408};
RX   PubMed=7399408; DOI=10.1515/bchm2.1980.361.1.875;
RA   Lill U., Pirzer P., Kukla D., Huber R., Eggerer H.;
RT   "Nicotinic acid metabolism enzymic preparation and absolute configuration
RT   of the substrate for 2,3-dimethylmalate lyase.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 361:875-884(1980).
CC   -!- FUNCTION: Catalyzes the formation of proponate and pyruvate from
CC       (2R,3S)-2,3-dimethylmalate. Has no activity toward dimethylmaleate,
CC       malate, citramalate, isocitrate and citrate.
CC       {ECO:0000269|PubMed:527937}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-2,3-dimethylmalate = propanoate + pyruvate;
CC         Xref=Rhea:RHEA:10472, ChEBI:CHEBI:15361, ChEBI:CHEBI:17272,
CC         ChEBI:CHEBI:57422; EC=4.1.3.32; Evidence={ECO:0000269|PubMed:527937,
CC         ECO:0000269|PubMed:7399408};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:16894175};
CC   -!- ACTIVITY REGULATION: Completely inhibited by propionic anhydride and by
CC       cystamine. Irreversibly inhibited by the mercapto reagents iodoacetate
CC       and iodoacetamide. Unaffected by hydroxylamine.
CC       {ECO:0000269|PubMed:527937}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.66 mM for 2,3-dimethylmalate {ECO:0000269|PubMed:527937};
CC   -!- PATHWAY: Cofactor degradation; nicotinate degradation; propanoate and
CC       pyruvate from 6-hydroxynicotinate: step 8/8.
CC       {ECO:0000269|PubMed:16894175}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16894175}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       {ECO:0000255}.
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DR   EMBL; DQ310789; ABC88406.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0QLE4; -.
DR   SMR; Q0QLE4; -.
DR   STRING; 1528.SAMN04488579_1126; -.
DR   KEGG; ag:ABC88406; -.
DR   BioCyc; MetaCyc:MON-11714; -.
DR   UniPathway; UPA01010; UER01019.
DR   GO; GO:0047529; F:2,3-dimethylmalate lyase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1901848; P:nicotinate catabolic process; IDA:UniProtKB.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; -; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   1: Evidence at protein level;
KW   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..289
FT                   /note="2,3-dimethylmalate lyase"
FT                   /id="PRO_0000403996"
SQ   SEQUENCE   289 AA;  31379 MW;  C155BC9C580389F3 CRC64;
     MNTAAKMREL LSTKKMVVAP GAHDAMTAKV IGRLGFDAVY MTGYGQSASH LGQPDVGLLT
     MTEMVARANA IVEAAGVPVI ADADTGFGNA VNVMRTVREY EKAGVAVIQL EDQVMPKKCG
     HMVGREIVSK EEMVGKIKAA VDTRVNPDFM IMARTDARTT KGIDEALERG LAYKEAGADI
     IFIESPEGEE EMKRINETIP GYTLANMVEG GRTPLLKNAE LEALGYNITI YPTASIYVAT
     KAMVDLWTAL KNDDTTAGVM DTMVTFSEFN DLMGLEKIRE VEHNYATGR