ID   CATB_ACIAD              Reviewed;         370 AA.
AC   Q43931; Q6FCA2;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Muconate cycloisomerase 1;
DE            EC=5.5.1.1 {ECO:0000250|UniProtKB:P08310};
DE   AltName: Full=Cis,cis-muconate lactonizing enzyme I;
DE            Short=MLE;
DE   AltName: Full=Muconate cycloisomerase I;
GN   Name=catB; OrderedLocusNames=ACIAD1446;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8125318; DOI=10.1016/0378-1119(94)90783-8;
RA   Shanley M.S., Harrison A., Parales R.E., Kowalchuk G., Mitchell D.J.,
RA   Ornston L.N.;
RT   "Unusual G + C content and codon usage in catIJF, a segment of the ben-cat
RT   supra-operonic cluster in the Acinetobacter calcoaceticus chromosome.";
RL   Gene 138:59-65(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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}.
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DR   EMBL; AF009224; AAC46430.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68309.1; -; Genomic_DNA.
DR   RefSeq; WP_011182286.1; NC_005966.1.
DR   AlphaFoldDB; Q43931; -.
DR   SMR; Q43931; -.
DR   STRING; 62977.ACIAD1446; -.
DR   EnsemblBacteria; CAG68309; CAG68309; ACIAD1446.
DR   GeneID; 45233858; -.
DR   KEGG; aci:ACIAD1446; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_4_5_6; -.
DR   OMA; MFGCYSD; -.
DR   OrthoDB; 951991at2; -.
DR   BioCyc; ASP62977:ACIAD_RS06680-MON; -.
DR   UniPathway; UPA00157; UER00259.
DR   Proteomes; UP000000430; Chromosome.
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;
KW   Reference proteome.
FT   CHAIN           1..370
FT                   /note="Muconate cycloisomerase 1"
FT                   /id="PRO_0000171248"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        303
FT                   /note="P -> A (in Ref. 1; AAC46430)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   370 AA;  40415 MW;  DC99E3B24EB91D8D CRC64;
     MYKSVETILV DIPTIRPHKL SVTTMQTQTL VLIKIITEDG IVGWGEATTI GGLNYGEESP
     ESVKANIDTY FKPLLLSIKA PLNVAQTLKL IRKSINGNRF AKCAIQTALL EIQAKRLNVP
     VSELLGGRIR DRLPVLWTLA SGDTDKDIAE AKKMIELKRH NTFKLKIGSN PLQHDVDHVI
     AIKKALGPEI SVRVDVNRAW SELECVKGIQ QLQDGGIDLI EQPCAIENTD ALARLTARFD
     VAIMADEVLT GPDSAYRIAK KSGADVFAVK VEQSGGLIEA CEVAKIARLA GISLYGGTML
     EGPVGSIASA HAFSTFETLE FGTELFGPLL LTQSILKTPL QYENFELVVP NTPGLGIEVD
     EDKLEQLRRH