CATB1_ACILW
ID CATB1_ACILW Reviewed; 379 AA.
AC O33946;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Muconate cycloisomerase 1-1;
DE EC=5.5.1.1 {ECO:0000250|UniProtKB:P08310};
DE AltName: Full=Cis,cis-muconate lactonizing enzyme I 1;
DE Short=MLE 1;
DE AltName: Full=Muconate cycloisomerase I 1;
GN Name=catB1;
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;
RX PubMed=9473520; DOI=10.1006/bbrc.1997.7912;
RA Kim S.I., Leem S.-H., Choi J.-S., Ha K.-S.;
RT "Organization and transcriptional characterization of the cat1 gene cluster
RT in Acinetobacter lwoffi K24.";
RL Biochem. Biophys. Res. Commun. 243:289-294(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 273-379.
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}.
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DR EMBL; U77658; AAC46226.1; -; Genomic_DNA.
DR PIR; JC5944; JC5944.
DR AlphaFoldDB; O33946; -.
DR SMR; O33946; -.
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..379
FT /note="Muconate cycloisomerase 1-1"
FT /id="PRO_0000171249"
FT ACT_SITE 169
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 40790 MW; 1152B582A6BFC417 CRC64;
MSSVTIERIE TCLVDLPTIR PHKLSVATMY GQTLMLVKVY CTDGAVGIGE GTTIAGMAYG
PESPEAMKLA IDAYFAPALV GKDATRIQTL MAHLGKLVKI NHFAKSALET ALLDAHGKRL
GVAVSELLGG RRRERLPVAW TLASGDTSRD IAEAEQMIEV RRHNVFKLKI GAKELKTDIK
HVAEIKRVVG EHAAVRVDVN MAWSETQAAW AIPALADAGC ELVEQPVASA AALARLMRRF
PVALMADEIL QGPDNAFEIA RVNGADVFAI KIEQSGGLFA AQRVAAIADA AGIELYGGTM
LEGAFSTVAS AHLFASFANL QWGTELFGPL LITEEILTKP LDYSDYQLTV PDGPGLGIEL
DEEKVRRFTR DGLIKVTKA