ID   CATB2_ACILW             Reviewed;         385 AA.
AC   O33949;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Muconate cycloisomerase 1-2;
DE            EC=5.5.1.1 {ECO:0000250|UniProtKB:P08310};
DE   AltName: Full=Cis,cis-muconate lactonizing enzyme I 2;
DE            Short=MLE 2;
DE   AltName: Full=Muconate cycloisomerase I 2;
GN   Name=catB2;
OS   Acinetobacter lwoffii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=28090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K24;
RA   Kim S.I., Leem S.-H., Choi J.S., Chung Y.H., Kim S., Park Y.-M., Ha K.-S.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-385.
RC   STRAIN=K24;
RX   PubMed=9260969; DOI=10.1128/jb.179.16.5226-5231.1997;
RA   Kim S.I., Leem S.-H., Choi J.-S., Chung Y.H., Kim S., Park Y.-M.,
RA   Park Y.K., Lee Y.N., Ha K.-S.;
RT   "Cloning and characterization of two catA genes in Acinetobacter lwoffii
RT   K24.";
RL   J. Bacteriol. 179:5226-5231(1997).
CC   -!- FUNCTION: Catalyzes a syn cycloisomerization.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-muconolactone = cis,cis-muconate + H(+);
CC         Xref=Rhea:RHEA:30031, ChEBI:CHEBI:15378, ChEBI:CHEBI:32379,
CC         ChEBI:CHEBI:58736; EC=5.5.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P08310};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-
CC       4,5-dihydro-2-furylacetate from catechol: step 2/3.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U77659; AAC31766.1; -; Genomic_DNA.
DR   PIR; T46824; T46824.
DR   AlphaFoldDB; O33949; -.
DR   SMR; O33949; -.
DR   UniPathway; UPA00157; UER00259.
DR   GO; GO:0018850; F:chloromuconate cycloisomerase activity; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0018849; F:muconate cycloisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
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.
FT   CHAIN           1..385
FT                   /note="Muconate cycloisomerase 1-2"
FT                   /id="PRO_0000171250"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   385 AA;  41138 MW;  A4DEC746C1D0CC51 CRC64;
     MIATPVKIES VETILVDVPT IRPHRLSVAT MNCQTLVLVR IRCADGVVGV GEGTTIGGLA
     YGEESPESIK VNIDTYFAPL LKGLDATRPG AAMATLRGLF QGNRFARSAV ETALFDAQAQ
     RLGVPLSELF GGRIRDSVDV AWTLASGDTT RDIDEAERVF EAKRHRVFKL KIGSRALADD
     VAHVVAIQKA LQGRGEVRVD VNQAWTESEA IWAGKRFADA SVALIEQPIA AENRAGLKRL
     TDLAQVPIMA DEALHGPADA FALASARAAD VFAVKIAQSG GLSGAANVAA IALAANIDLY
     GGTMLEGAVG TIASAQLFST FGELKWGTEL FGPLLLTEEI LTEPLRYENF VLHLPQGPGL
     GITLDWDKID RLRRDTRKGA SITMN