ID   TFDD1_CUPPJ             Reviewed;         370 AA.
AC   P05404; Q46M67;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 4.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Chloromuconate cycloisomerase;
DE            EC=5.5.1.7;
DE   AltName: Full=Muconate cycloisomerase II;
GN   Name=tfdDI; Synonyms=tfdD; OrderedLocusNames=Reut_D6465;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OG   Plasmid pJP4, and Plasmid pPJ4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pJP4;
RX   PubMed=2185214; DOI=10.1128/jb.172.5.2351-2359.1990;
RA   Perkins E.J., Gordon M.P., Caceres O., Lurquin P.F.;
RT   "Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase
RT   and dichlorocatechol oxidative operons of plasmid pJP4.";
RL   J. Bacteriol. 172:2351-2359(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pJP4;
RX   PubMed=2583528; DOI=10.1016/0378-1119(89)90108-x;
RA   Ghosal D., You I.-S.;
RT   "Operon structure and nucleotide homology of the chlorocatechol oxidation
RT   genes of plasmids pJP4 and pAC27.";
RL   Gene 83:225-232(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pJP4;
RX   PubMed=15186344; DOI=10.1111/j.1462-2920.2004.00596.x;
RA   Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T.,
RA   Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B.;
RT   "Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha
RT   JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants
RT   and evolution of specialized chloroaromatic degradation pathways.";
RL   Environ. Microbiol. 6:655-668(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197; PLASMID=pPJ4;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-166.
RC   PLASMID=pJP4;
RX   PubMed=3405772; DOI=10.1093/nar/16.14.7200;
RA   Perkins E.J., Bolton G., Gordon M.P., Lurquin P.F.;
RT   "Partial nucleotide sequence of the chlorocatechol degradative operon
RT   tfdCDEF of pJP4 and similarity to promoters of the chlorinated aromatic
RT   degradative operons tfdA and clcABD.";
RL   Nucleic Acids Res. 16:7200-7200(1988).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS.
RC   PLASMID=pJP4;
RX   PubMed=15299479; DOI=10.1107/s090744499300900x;
RA   Hoier H., Schloemann M., Hammer A., Glusker J.P., Carrell H.L., Goldman A.,
RA   Stezowski J.J., Heinemann U.;
RT   "Crystal structure of chloromuconate cycloisomerase from Alcaligenes
RT   eutrophus JMP134 (pJP4) at 3-A resolution.";
RL   Acta Crystallogr. D 50:75-84(1994).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RC   PLASMID=pJP4;
RX   PubMed=15299651; DOI=10.1107/s0907444995008936;
RA   Kleywegt G.J., Jones T.A.;
RT   "A re-evaluation of the crystal structure of chloromuconate
RT   cycloisomerase.";
RL   Acta Crystallogr. D 52:858-863(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3-chloro-
CC         cis,cis-muconate + H(+); Xref=Rhea:RHEA:11032, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17589, ChEBI:CHEBI:85538; EC=5.5.1.7;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- PATHWAY: Aromatic compound metabolism; 3-chlorocatechol degradation.
CC   -!- MISCELLANEOUS: Chloromuconate cycloisomerase II is highly active toward
CC       chlorinated substrates but retains diminished activity toward the non-
CC       chlorinated substrates.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. {ECO:0000305}.
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DR   EMBL; M35097; AAA98263.1; -; Genomic_DNA.
DR   EMBL; M31458; AAA98267.1; -; Genomic_DNA.
DR   EMBL; AY365053; AAR31038.1; -; Genomic_DNA.
DR   EMBL; CP000093; AAZ65763.1; -; Genomic_DNA.
DR   PIR; B35255; B35255.
DR   RefSeq; WP_011178385.1; NZ_AY365053.1.
DR   PDB; 2CHR; X-ray; 3.00 A; A=1-370.
DR   PDBsum; 2CHR; -.
DR   AlphaFoldDB; P05404; -.
DR   SMR; P05404; -.
DR   GeneID; 55536835; -.
DR   KEGG; reu:Reut_D6465; -.
DR   HOGENOM; CLU_030273_4_5_4; -.
DR   OrthoDB; 5596677at2; -.
DR   BioCyc; MetaCyc:MONOMER-14403; -.
DR   UniPathway; UPA00083; -.
DR   EvolutionaryTrace; P05404; -.
DR   GO; GO:0018850; F:chloromuconate cycloisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0018849; F:muconate cycloisomerase activity; IEA:InterPro.
DR   GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd03318; MLE; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   InterPro; IPR013370; Chloromuconate_cycloisomerase.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   NCBIfam; TIGR02534; mucon_cyclo; 1.
DR   PANTHER; PTHR48073:SF2; O-SUCCINYLBENZOATE SYNTHASE; 1.
DR   PANTHER; PTHR48073; O-SUCCINYLBENZOATE SYNTHASE-RELATED; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDG01258; (chloro)muconate_cycloisomeras; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00908; MR_MLE_1; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism; Isomerase; Manganese;
KW   Metal-binding; Plasmid.
FT   CHAIN           1..370
FT                   /note="Chloromuconate cycloisomerase"
FT                   /id="PRO_0000171256"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        323
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         245
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   CONFLICT        306..325
FT                   /note="SVALQLYSTVPSLPFGCELI -> RLHSAYLRFHASVRLRTV (in Ref.
FT                   2; AAA98267)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..20
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   STRAND          25..38
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   TURN            51..55
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           60..70
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           72..75
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           83..91
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           98..115
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           120..123
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   STRAND          130..138
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           143..155
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   STRAND          161..165
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           171..184
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   TURN            185..188
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   STRAND          189..194
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           202..212
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   TURN            213..215
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   STRAND          218..220
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           228..237
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   STRAND          239..247
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           251..258
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   TURN            259..261
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   STRAND          264..266
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           270..273
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           276..289
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           302..312
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           326..329
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   STRAND          334..336
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   STRAND          343..347
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   STRAND          351..353
FT                   /evidence="ECO:0007829|PDB:2CHR"
FT   HELIX           360..366
FT                   /evidence="ECO:0007829|PDB:2CHR"
SQ   SEQUENCE   370 AA;  39722 MW;  C08032835D42EBDD CRC64;
     MKIDAIEAVI VDVPTKRPIQ MSITTVHQQS YVIVRVYSEG LVGVGEGGSV GGPVWSAECA
     ETIKIIVERY LAPHLLGTDA FNVSGALQTM ARAVTGNASA KAAVEMALLD LKARALGVSI
     AELLGGPLRS AIPIAWTLAS GDTKRDLDSA VEMIERRRHN RFKVKLGFRS PQDDLIHMEA
     LSNSLGSKAY LRVDVNQAWD EQVASVYIPE LEALGVELIE QPVGRENTQA LRRLSDNNRV
     AIMADESLST LASAFDLARD RSVDVFSLKL CNMGGVSATQ KIAAVAEASG IASYGGTMLD
     STIGTSVALQ LYSTVPSLPF GCELIGPFVL ADTLSHEPLE IRDYELQVPT GVGHGMTLDE
     DKVRQYARVS
//