TCBD_PSESQ
ID TCBD_PSESQ Reviewed; 370 AA.
AC P27099;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Chloromuconate cycloisomerase;
DE EC=5.5.1.7;
DE AltName: Full=Muconate cycloisomerase II;
GN Name=tcbD;
OS Pseudomonas sp. (strain P51).
OG Plasmid pP51.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=65067;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2013566; DOI=10.1128/jb.173.8.2425-2434.1991;
RA van der Meer J.R., Eggen R.I., Zehnder A.J., de Vos W.M.;
RT "Sequence analysis of the Pseudomonas sp. strain P51 tcb gene cluster,
RT which encodes metabolism of chlorinated catechols: evidence for
RT specialization of catechol 1,2-dioxygenases for chlorinated substrates.";
RL J. Bacteriol. 173:2425-2434(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), AND COFACTOR.
RX PubMed=12930985; DOI=10.1110/ps.0388503;
RA Kajander T., Lehtioe L., Schloemann M., Goldman A.;
RT "The structure of Pseudomonas P51 Cl-muconate lactonizing enzyme: co-
RT evolution of structure and dynamics with the dehalogenation function.";
RL Protein Sci. 12:1855-1864(2003).
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 Evidence={ECO:0000269|PubMed:12930985};
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; M57629; AAD13626.1; -; Genomic_DNA.
DR PIR; B43673; B43673.
DR PDB; 1NU5; X-ray; 1.95 A; A=1-370.
DR PDBsum; 1NU5; -.
DR AlphaFoldDB; P27099; -.
DR SMR; P27099; -.
DR KEGG; ag:AAD13626; -.
DR BioCyc; MetaCyc:MON-14405; -.
DR UniPathway; UPA00083; -.
DR EvolutionaryTrace; P27099; -.
DR GO; GO:0018850; F:chloromuconate cycloisomerase activity; NAS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0018849; F:muconate cycloisomerase activity; IEA:InterPro.
DR GO; GO:0046300; P:2,4-dichlorophenoxyacetic acid catabolic process; NAS:UniProtKB.
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_0000171254"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT ACT_SITE 323
FT /note="Proton donor"
FT BINDING 194
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
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 STRAND 2..21
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 24..38
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:1NU5"
FT TURN 51..55
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 201..214
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 302..312
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1NU5"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:1NU5"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:1NU5"
SQ SEQUENCE 370 AA; 39487 MW; 8C6ADA522C63508A CRC64;
MKIEAISTTI VDVPTRRPLQ MSFTTVHKQS YVIVQVKAGG LVGIGEGGSV GGPTWGSESA
ETIKVIIDNY LAPLLVGKDA SNLSQARVLM DRAVTGNLSA KAAIDIALHD LKARALNLSI
ADLIGGTMRT SIPIAWTLAS GDTARDIDSA LEMIETRRHN RFKVKLGART PAQDLEHIRS
IVKAVGDRAS VRVDVNQGWD EQTASIWIPR LEEAGVELVE QPVPRANFGA LRRLTEQNGV
AILADESLSS LSSAFELARD HAVDAFSLKL CNMGGIANTL KVAAVAEAAG ISSYGGTMLD
STVGTAAALH VYATLPSLPY GCELIGPWVL GDRLTQQDLE IKDFEVHLPL GSGLGVDLDH
DKVRHYTRAA
