TFDD_DELAC
ID TFDD_DELAC Reviewed; 370 AA.
AC Q9RNZ9; Q93T14; Q9WXC9;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Chloromuconate cycloisomerase;
DE EC=5.5.1.7;
GN Name=tfdD;
OS Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=80866;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=P4a;
RX PubMed=12949179; DOI=10.1099/mic.0.26260-0;
RA Hoffmann D., Kleinsteuber S., Mueller R.H., Babel W.;
RT "A transposon encoding the complete 2,4-dichlorophenoxyacetic acid
RT degradation pathway in the alkalitolerant strain Delftia acidovorans P4a.";
RL Microbiology 149:2545-2556(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 67-268.
RC STRAIN=P4a;
RA Hoffmann D., Kleinsteuber S., Mueller R.H., Babel W.;
RT "Development and application of PCR primers for the detection of the tfd
RT genes in Delftia acidovorans P4a involved in the degradation of 2,4-D.";
RL Acta Biotechnol. 21:321-331(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-263.
RC STRAIN=MC1;
RX PubMed=11572451; DOI=10.1078/0944-5013-00089;
RA Mueller R.H., Kleinsteuber S., Babel W.;
RT "Physiological and genetic characteristics of two bacterial strains
RT utilizing phenoxypropionate and phenoxyacetate herbicides.";
RL Microbiol. Res. 156:121-131(2001).
RN [4]
RP PROTEIN SEQUENCE OF 1-16, AND INDUCTION BY 2,4-DCPP.
RC STRAIN=MC1;
RX PubMed=15073309; DOI=10.1099/mic.0.26774-0;
RA Benndorf D., Davidson I., Babel W.;
RT "Regulation of catabolic enzymes during long-term exposure of Delftia
RT acidovorans MC1 to chlorophenoxy herbicides.";
RL Microbiology 150:1005-1014(2004).
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 -!- INDUCTION: By 2,4-dichlorophenoxypropionic acid (2,4-DCPP).
CC {ECO:0000269|PubMed:15073309}.
CC -!- MISCELLANEOUS: Different ratios of isoforms are detectable, depending
CC on concentration of dichlorprop.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000305}.
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DR EMBL; AY078159; AAK57008.2; -; Genomic_DNA.
DR EMBL; AF176244; AAD55083.1; -; Genomic_DNA.
DR RefSeq; WP_011255151.1; NC_019283.1.
DR RefSeq; YP_006961882.1; NC_019283.1.
DR AlphaFoldDB; Q9RNZ9; -.
DR SMR; Q9RNZ9; -.
DR UniPathway; UPA00083; -.
DR PRO; PR:Q9RNZ9; -.
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 Aromatic hydrocarbons catabolism; Direct protein sequencing; Isomerase;
KW Manganese; Metal-binding.
FT CHAIN 1..370
FT /note="Chloromuconate cycloisomerase"
FT /id="PRO_0000171258"
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"
SQ SEQUENCE 370 AA; 39465 MW; 195D3101CA18B31C CRC64;
MKIEAISTTI VDVPTRRPLQ MSFTTVHKQS YVIVQVTAGG LVGIGEGGSV GGPTWGSESA
ETIKVIIDNY LAPLLIGKDA SNLSEARALM DRAVTGNLSA KAAIDIALHD LKARALNLSI
ADLIGGTMRK SIPIAWTLAS GDTARDIDSA LEMIEARRHN RFKVKLGART PAQDLEHIRS
IVKAVGDKAS VRVDVNQGWD EQTASIWIPR LEEAGVELVE QPVPRANFGA LRRLTEQNGV
AILADESLSS LSSAFELARD RAVDAFSLKL CNMGGIANTL KVAAIAEAAG ISSYGGTMLD
STVGTAAALH VYATLPSLPY GCELIGPWVL SDRLTQQDLE IKDFEVHLPV GSGLGVDLDH
DKVRHYTRAA
