ID   MCT_CHLAA               Reviewed;         409 AA.
AC   A9WC36;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=2-methylfumaryl-CoA isomerase;
DE            EC=5.4.1.3;
GN   Name=mct; OrderedLocusNames=Caur_0175;
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, INDUCTION, AND SUBUNIT.
RC   STRAIN=DSM 636 / Ok-70-fl;
RX   PubMed=19955419; DOI=10.1073/pnas.0908356106;
RA   Zarzycki J., Brecht V., Muller M., Fuchs G.;
RT   "Identifying the missing steps of the autotrophic 3-hydroxypropionate CO2
RT   fixation cycle in Chloroflexus aurantiacus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:21317-21322(2009).
CC   -!- FUNCTION: Involved in the glyoxylate assimilation cycle used to
CC       regenerate acetyl-CoA and produce pyruvate as universal precursor for
CC       biosynthesis. This reaction involves an intramolecular CoA transferase
CC       that catalyzes the reversible transfer of the CoA moiety from the C1-
CC       carboxyl group of mesaconyl-CoA to the C4-carboxyl group. It does not
CC       require free mesaconate as CoA acceptor. {ECO:0000269|PubMed:19955419}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylfumaryl-CoA = 3-methylfumaryl-CoA;
CC         Xref=Rhea:RHEA:38267, ChEBI:CHEBI:75635, ChEBI:CHEBI:75636;
CC         EC=5.4.1.3; Evidence={ECO:0000269|PubMed:19955419};
CC   -!- ACTIVITY REGULATION: Partially inhibited by hydroxylamine.
CC       {ECO:0000269|PubMed:19955419}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=240 uM for 2-methylfumaryl-CoA {ECO:0000269|PubMed:19955419};
CC         Vmax=520 umol/min/mg enzyme {ECO:0000269|PubMed:19955419};
CC         Note=kcat is 840 sec(-1) for isomerase activity with 2-methylfumaryl-
CC         CoA.;
CC       pH dependence:
CC         Optimum pH is between 7.5 and 7.8. {ECO:0000269|PubMed:19955419};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.
CC         {ECO:0000269|PubMed:19955419};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19955419}.
CC   -!- INDUCTION: Under autotrophic growth conditions.
CC       {ECO:0000269|PubMed:19955419}.
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family. Mesaconyl-CoA
CC       isomerase subfamily. {ECO:0000305}.
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DR   EMBL; CP000909; ABY33429.1; -; Genomic_DNA.
DR   RefSeq; WP_012256085.1; NC_010175.1.
DR   RefSeq; YP_001633818.1; NC_010175.1.
DR   AlphaFoldDB; A9WC36; -.
DR   SMR; A9WC36; -.
DR   STRING; 324602.Caur_0175; -.
DR   EnsemblBacteria; ABY33429; ABY33429; Caur_0175.
DR   KEGG; cau:Caur_0175; -.
DR   PATRIC; fig|324602.8.peg.202; -.
DR   eggNOG; COG1804; Bacteria.
DR   HOGENOM; CLU_033975_0_1_0; -.
DR   OMA; YRRWPLT; -.
DR   BioCyc; MetaCyc:MON-17293; -.
DR   BRENDA; 5.4.1.3; 1352.
DR   Proteomes; UP000002008; Chromosome.
DR   GO; GO:0016867; F:intramolecular transferase activity, transferring acyl groups; IDA:UniProtKB.
DR   GO; GO:0043427; P:carbon fixation by 3-hydroxypropionate cycle; IDA:UniProtKB.
DR   Gene3D; 3.30.1540.10; -; 1.
DR   Gene3D; 3.40.50.10540; -; 1.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR   InterPro; IPR026347; Mesacon_CoA_Isoase.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 1.
DR   TIGRFAMs; TIGR04253; mesacon_CoA_iso; 1.
PE   1: Evidence at protein level;
KW   Carbon dioxide fixation; Isomerase; Reference proteome.
FT   CHAIN           1..409
FT                   /note="2-methylfumaryl-CoA isomerase"
FT                   /id="PRO_0000429583"
FT   ACT_SITE        165
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  44813 MW;  16778460EA9CC9DF CRC64;
     MKGILHGLRV VEGSAFVAAP LGGMTLAQLG ADVIRFDPIG GGLDYKRWPV TLDGKHSLFW
     AGLNKGKRSI AIDIRHPRGQ ELLTQLICAP GEHAGLFITN FPARGWLSYD ELKRHRADLI
     MVNLVGRRDG GSEVDYTVNP QLGLPFMTGP VTTPDVVNHV LPAWDIVTGQ MIALGLLAAE
     RHRRLTGEGQ LVKIALKDVG LAMIGHLGMI AEVMINDTDR PRQGNYLYGA FGRDFETLDG
     KRVMVVGLTD LQWKALGKAT GLTDAFNALG ARLGLNMDEE GDRFRARHEI AALLEPWFHA
     RTLAEVRRIF EQHRVTWAPY RTVREAIAQD PDCSTDNPMF AMVEQPGIGS YLMPGSPLDF
     TAVPRLPVQP APRLGEHTDE ILLEVLGLSE AEVGRLHDEG IVAGPDRAA