ID   CLCB_PSEPU              Reviewed;         370 AA.
AC   P11452; P15741;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Chloromuconate cycloisomerase;
DE            EC=5.5.1.7;
DE   AltName: Full=Muconate cycloisomerase II;
GN   Name=clcB;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid pAC27.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3299368; DOI=10.1073/pnas.84.13.4460;
RA   Frantz B., Chakrabarty A.M.;
RT   "Organization and nucleotide sequence determination of a gene cluster
RT   involved in 3-chlorocatechol degradation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:4460-4464(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3609743; DOI=10.1016/0378-1119(87)90045-x;
RA   Aldrich T.L., Frantz B., Gill J.F., Kilbane J.J., Chakrabarty A.M.;
RT   "Cloning and complete nucleotide sequence determination of the catB gene
RT   encoding cis,cis-muconate lactonizing enzyme.";
RL   Gene 52:185-195(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AC867;
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).
CC   -!- FUNCTION: Highly active toward chlorinated substrates but retains
CC       diminished activity toward the non-chlorinated substrates.
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; Evidence={ECO:0000250};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-chlorocatechol degradation.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. {ECO:0000305}.
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DR   EMBL; M16964; AAA98282.1; -; Genomic_DNA.
DR   EMBL; M31457; AAA98260.1; -; Genomic_DNA.
DR   PIR; JQ0176; JQ0176.
DR   AlphaFoldDB; P11452; -.
DR   SMR; P11452; -.
DR   UniPathway; UPA00083; -.
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:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR   CDD; cd03318; MLE; 1.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 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   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDG01258; (chloro)muconate_cycloisomeras; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
DR   TIGRFAMs; TIGR02534; mucon_cyclo; 1.
DR   PROSITE; PS00908; MR_MLE_1; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Isomerase; Manganese; Metal-binding;
KW   Plasmid.
FT   CHAIN           1..370
FT                   /note="Chloromuconate cycloisomerase"
FT                   /id="PRO_0000171253"
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                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        42
FT                   /note="V -> C (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114
FT                   /note="R -> H (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   370 AA;  39847 MW;  9279DD393F42BBCD CRC64;
     MKIEAIDVTL VDVPASRPIQ MSFTTVQKQS YAIVQIRAGG LVGIGEGSSV GGPTWSSECA
     ETIKVIIETY LAPLLIGKDA TNLRELQHLM ERAVTGNYSA KAAIDVALHD LKARSLNLPL
     SDLIGGAIQQ GIPIAWTLAS GDTQRDIAIA EEMIERRRHN RFKIKLGVRS PADDLRHIEK
     IIERVGDRAA VRVDINQAWD ENTASVWIPR LEAAGVELVE QPVARSNFDA LRRLSADNGV
     AILADESLSS LASAFELARH HCVDAFSLKL CNMGGVANTL KVAAIAEASG IASYGGTMLD
     SSIGTAAALH VYATLPTMPF ECELLGPWVL ADTLTQTQLE IKDFEIRLPS GPGLGVDIDP
     DKLRHFTRAG