TFDD2_CUPPJ
ID TFDD2_CUPPJ Reviewed; 372 AA.
AC P42428; Q46M58; Q6UP90;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Chloromuconate cycloisomerase;
DE EC=5.5.1.7;
DE AltName: Full=Muconate cycloisomerase II;
GN Name=tfdDII; Synonyms=tfdD2; OrderedLocusNames=Reut_D6474;
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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-234.
RC PLASMID=pJP4;
RX PubMed=8157603; DOI=10.1128/jb.176.8.2348-2353.1994;
RA Matrubutham U., Harker A.R.;
RT "Analysis of duplicated gene sequences associated with tfdR and tfdS in
RT Alcaligenes eutrophus JMP134.";
RL J. Bacteriol. 176:2348-2353(1994).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA65064.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAZ65772.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY365053; AAR31047.1; -; Genomic_DNA.
DR EMBL; CP000093; AAZ65772.1; ALT_INIT; Genomic_DNA.
DR EMBL; M98445; AAA65064.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; P42428; -.
DR SMR; P42428; -.
DR EnsemblBacteria; AAZ65772; AAZ65772; Reut_D6474.
DR KEGG; reu:Reut_D6474; -.
DR HOGENOM; CLU_030273_4_5_4; -.
DR OMA; RQRDICL; -.
DR BioCyc; MetaCyc:MON-14413; -.
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.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Isomerase; Manganese; Metal-binding;
KW Plasmid.
FT CHAIN 1..372
FT /note="Chloromuconate cycloisomerase"
FT /id="PRO_0000171257"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 316
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CONFLICT 65
FT /note="A -> G (in Ref. 3; AAA65064)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="A -> D (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..201
FT /note="LEGKASLRVDPNEAWDEPTTMRAL -> TRGQDEPAPSIPTKRGTSRPRCGT
FT (in Ref. 3; AAA65064)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..211
FT /note="GVEI -> AWKF (in Ref. 3; AAA65064)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 40045 MW; 7D170C1364D04140 CRC64;
MIVDLPLRRI QQFARLGAKH QSSVLIRLHT KGGIVGIGES ITPCGPWWSG DSVEAIQATI
NHYLAPLVVG EPALDASRIM AKLHGRVAGN AFAKAGIEMA LLDAVGKIVD APIHVLLGGR
FRDRLSVAWP LATGDVNQEV DEAFRMLEAG KAGAFKLKMG ALPLAQDLRR ALAIAKELEG
KASLRVDPNE AWDEPTTMRA LAPLEAAGVE IIEQPVARWN LDAMARIHRQ ARSMLLIDEG
VQSLHDASEV VKRAAAGLVS LKIMKTGGMR PARAMADIAN AGGMHVYMGT FLETSIGTAA
NMQLAASIES LPYGGEVIGP LLIEEDLCEV PAVYKEHALW LPEGPGLGIR LDENQVRRFA
RASSQRIDRH SA
