MII_EUBBA
ID MII_EUBBA Reviewed; 380 AA.
AC Q0QLE6;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=3-methylitaconate isomerase;
DE EC=5.3.3.6;
DE AltName: Full=(R)-3-methylitaconate isomerase {ECO:0000303|PubMed:16894175};
DE AltName: Full=3-methylitaconate delta-isomerase;
GN Name=mii;
OS Eubacterium barkeri (Clostridium barkeri).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1528;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC88404.1}
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:ABC88404.1};
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, ACTIVITY REGULATION, INDUCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=5574401; DOI=10.1016/s0021-9258(18)62235-5;
RA Kung H.F., Stadtman T.C.;
RT "Nicotinic acid metabolism. VI. Purification and properties of alpha-
RT methyleneglutarate mutase (B 12-dependent) and methylitaconate isomerase.";
RL J. Biol. Chem. 246:3378-3388(1971).
RN [3] {ECO:0000305}
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC 5359 {ECO:0000269|PubMed:2776761};
RX PubMed=2776761; DOI=10.1111/j.1432-1033.1989.tb14995.x;
RA Michel C., Hartrampf G., Buckel W.;
RT "Assay and purification of the adenosylcobalamin-dependent 2-
RT methyleneglutarate mutase from Clostridium barkeri.";
RL Eur. J. Biochem. 184:103-107(1989).
RN [4] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=19559030; DOI=10.1016/j.jmb.2009.06.052;
RA Velarde M., Macieira S., Hilberg M., Broker G., Tu S.M., Golding B.T.,
RA Pierik A.J., Buckel W., Messerschmidt A.;
RT "Crystal structure and putative mechanism of 3-methylitaconate-delta-
RT isomerase from Eubacterium barkeri.";
RL J. Mol. Biol. 391:609-620(2009).
CC -!- FUNCTION: Catalyzes the reversible isomerization of (R)-3-
CC methylitaconate to 2,3-dimethylmaleate. Has very low isomerase activity
CC with itaconate. {ECO:0000269|PubMed:19559030}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylene-3-methylsuccinate = dimethylmaleate;
CC Xref=Rhea:RHEA:23480, ChEBI:CHEBI:17081, ChEBI:CHEBI:57637;
CC EC=5.3.3.6; Evidence={ECO:0000269|PubMed:19559030,
CC ECO:0000269|PubMed:2776761, ECO:0000269|PubMed:5574401};
CC -!- ACTIVITY REGULATION: Inhibited by oxidized glutathione, p-
CC chloromercuriphenylsulfonic acid and iodoacetic acid. Not inhibited by
CC the chelating agent alpha,alpha-dipyridyl. Activity is slightly
CC increased by EDTA. Not activated by Fe(2+), Mg(2+), Mn(2+) or Ca(2+).
CC Unaffected by K(+), Na(+), NH4(+), Rb(+) or Li(+).
CC {ECO:0000269|PubMed:5574401}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 mM for (R,S)-3-methylitaconate {ECO:0000269|PubMed:19559030,
CC ECO:0000269|PubMed:5574401};
CC KM=60 mM for itaconate {ECO:0000269|PubMed:19559030,
CC ECO:0000269|PubMed:5574401};
CC pH dependence:
CC Optimum pH is 6.8-8.2. {ECO:0000269|PubMed:19559030,
CC ECO:0000269|PubMed:5574401};
CC -!- PATHWAY: Cofactor degradation; nicotinate degradation; propanoate and
CC pyruvate from 6-hydroxynicotinate: step 6/8.
CC {ECO:0000269|PubMed:16894175}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19559030,
CC ECO:0000269|PubMed:2776761}.
CC -!- INDUCTION: By nicotinate. {ECO:0000269|PubMed:5574401}.
CC -!- SIMILARITY: Belongs to the PrpF family. {ECO:0000305}.
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DR EMBL; DQ310789; ABC88404.1; -; Genomic_DNA.
DR PDB; 3G7K; X-ray; 2.70 A; A/B/C/D=1-380.
DR PDBsum; 3G7K; -.
DR AlphaFoldDB; Q0QLE6; -.
DR SMR; Q0QLE6; -.
DR STRING; 1528.SAMN04488579_1128; -.
DR KEGG; ag:ABC88404; -.
DR BioCyc; MetaCyc:MON-11717; -.
DR BRENDA; 5.3.3.6; 1459.
DR UniPathway; UPA01010; UER01017.
DR EvolutionaryTrace; Q0QLE6; -.
DR GO; GO:0050100; F:methylitaconate delta-isomerase activity; IDA:UniProtKB.
DR GO; GO:1901848; P:nicotinate catabolic process; IDA:UniProtKB.
DR InterPro; IPR007400; PrpF_protein.
DR PANTHER; PTHR43709; PTHR43709; 1.
DR Pfam; PF04303; PrpF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase.
FT CHAIN 1..380
FT /note="3-methylitaconate isomerase"
FT /id="PRO_0000404092"
FT STRAND 4..14
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:3G7K"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3G7K"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3G7K"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3G7K"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:3G7K"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3G7K"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3G7K"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 194..210
FT /evidence="ECO:0007829|PDB:3G7K"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3G7K"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:3G7K"
FT HELIX 228..244
FT /evidence="ECO:0007829|PDB:3G7K"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 259..269
FT /evidence="ECO:0007829|PDB:3G7K"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:3G7K"
FT HELIX 305..316
FT /evidence="ECO:0007829|PDB:3G7K"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 354..362
FT /evidence="ECO:0007829|PDB:3G7K"
FT STRAND 364..375
FT /evidence="ECO:0007829|PDB:3G7K"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:3G7K"
SQ SEQUENCE 380 AA; 40273 MW; 6D37CCBC1CD128D9 CRC64;
MSDQMRIPCV IMRAGTSKGI FLKGNDLPAD QELRDKVILR IFGSPDVRQI DGLAGADPLT
SKLAIIGPST HPDADVDYTF AQVSITDAVV DYNGNCGNIS AGVGPFAIDE SFVKAVEPMT
RVCIHNTNTG KLLYAEVEVE DGKAKVSGDC KIDGVPGTNA PELMDFSDTA GAATGKVLPT
GNVVDVLSTS KGDIDVSIVD VANPCIFVHA KDVNMTGTET PDVINGNADL LAYLEEIRAK
CCVKIGMAAT EKEASEKSPA FPMIAFVTKP EDYVDFSTGN TISGDDVDLV SRLMFMQVLH
KTYAGTATAC TGSAARIPGT IVNQVLRDTG DEDTVRIGHP AGVIPVVSIV KDGKVEKAAL
IRTARRIMEG YVYVEKAKLV
