DMDA_EUBBA
ID DMDA_EUBBA Reviewed; 420 AA.
AC Q0QLE2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=2,3-dimethylmalate dehydratase large subunit {ECO:0000303|PubMed:16894175};
DE EC=4.2.1.85;
GN Name=dmdA;
OS Eubacterium barkeri (Clostridium barkeri).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1528;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC88408.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC 5359 {ECO:0000312|EMBL:ABC88408.1};
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 CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC 5359 {ECO:0000269|PubMed:6489933};
RX PubMed=6489933; DOI=10.1515/bchm2.1984.365.2.847;
RA Kollmann-Koch A., Eggerer H.;
RT "Nicotinic acid metabolism. Dimethylmaleate hydratase.";
RL Hoppe-Seyler's Z. Physiol. Chem. 365:847-857(1984).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-2,3-dimethylmalate = dimethylmaleate + H2O;
CC Xref=Rhea:RHEA:20253, ChEBI:CHEBI:15377, ChEBI:CHEBI:17081,
CC ChEBI:CHEBI:57422; EC=4.2.1.85;
CC Evidence={ECO:0000269|PubMed:6489933};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:A6LPX4,
CC ECO:0000255|HAMAP-Rule:MF_01027};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:A6LPX4, ECO:0000255|HAMAP-Rule:MF_01027};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.1 mM for dimethylmaleate {ECO:0000269|PubMed:6489933};
CC pH dependence:
CC Highly active between pH 6.5 and 9.0. Retains 50% and 10% of maximum
CC activity at pH 5.0 and 4.5, respectively.
CC {ECO:0000269|PubMed:6489933};
CC -!- PATHWAY: Cofactor degradation; nicotinate degradation; propanoate and
CC pyruvate from 6-hydroxynicotinate: step 7/8.
CC {ECO:0000269|PubMed:16894175}.
CC -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC {ECO:0000250|UniProtKB:A6LPX4}.
CC -!- INDUCTION: By nicotinic acid. {ECO:0000269|PubMed:6489933}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01027}.
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DR EMBL; DQ310789; ABC88408.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0QLE2; -.
DR SMR; Q0QLE2; -.
DR STRING; 1528.SAMN04488579_1124; -.
DR KEGG; ag:ABC88408; -.
DR BioCyc; MetaCyc:MON-13676; -.
DR UniPathway; UPA01010; UER01018.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0047868; F:dimethylmaleate hydratase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:1901848; P:nicotinate catabolic process; IDA:UniProtKB.
DR CDD; cd01583; IPMI; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR HAMAP; MF_01027; LeuC_type2; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR InterPro; IPR033941; IPMI_cat.
DR InterPro; IPR011823; IsopropMal_deHydtase_lsu_bac.
DR Pfam; PF00330; Aconitase; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR01343; hacA_fam; 1.
DR TIGRFAMs; TIGR02086; IPMI_arch; 1.
DR TIGRFAMs; TIGR02083; LEU2; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding.
FT CHAIN 1..420
FT /note="2,3-dimethylmalate dehydratase large subunit"
FT /id="PRO_0000403994"
FT BINDING 301
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:A6LPX4, ECO:0000255|HAMAP-
FT Rule:MF_01027"
FT BINDING 361
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:A6LPX4, ECO:0000255|HAMAP-
FT Rule:MF_01027"
FT BINDING 364
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:A6LPX4, ECO:0000255|HAMAP-
FT Rule:MF_01027"
SQ SEQUENCE 420 AA; 44821 MW; 7A709C21B776B48C CRC64;
MGMTMTQKIL AAHASLDSVK AGDLIMADLD MVLANDITGP VAINVFGTID KEKVFDKDKI
ALVPDHFAPA KDIKSAQQCK QVRCFACDQE ITNYFEIGEM GIEHALLPEK GLVAAGDVVI
GADSHTCTYG ALGAFSTGVG STDMAVGMAT GKAWFKVPAA LRFNLTGTLN KNVSGKDLIL
HIIGMIGVDG ALYRSMEFTG PGVACLSMDD RFTISNMAIE AGGKNGIFPV DDQTISYMEE
HGSGDYKVYA ADADAVYEKT FDIDLSQLKS TVAFPHLPEN TKTVDAIEEP VTIDQVVIGS
CTNGRFEDLK RAADILRGKH VKKGVRMLVI PATHKIYLDA MEAGYLREFI EAGATISTPT
CGPCLGGYMG ILAEGERCVS TTNRNFVGRM GHVDSEVYLA SPEVAAASAI LGRIATPDEL
