TFDD1_CUPPJ
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 03-AUG-2022, entry version 166.
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; Proteobacteria; 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 EnsemblBacteria; AAZ65763; AAZ65763; Reut_D6465.
DR GeneID; 55536835; -.
DR KEGG; reu:Reut_D6465; -.
DR HOGENOM; CLU_030273_4_5_4; -.
DR OMA; HEEFPVT; -.
DR OrthoDB; 951991at2; -.
DR BioCyc; MetaCyc:MON-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: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 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
