CATB_PSEPU
ID CATB_PSEPU Reviewed; 375 AA.
AC P08310;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Muconate cycloisomerase 1;
DE EC=5.5.1.1 {ECO:0000269|PubMed:5330966};
DE AltName: Full=Cis,cis-muconate lactonizing enzyme I;
DE Short=MLE;
DE AltName: Full=Muconate cycloisomerase I;
GN Name=catB;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PRS2015;
RX PubMed=3609743; DOI=10.1016/0378-1119(87)90045-x;
RA Aldrich T.L., Frantz B., Gill J.F., Kilbane J.J., Chakrabarty A.M.;
RT "Cloning and complete nucleotide sequence determination of the catB gene
RT encoding cis,cis-muconate lactonizing enzyme.";
RL Gene 52:185-195(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2449420; DOI=10.1128/jb.170.3.1297-1304.1988;
RA Aldrich T.L., Chakrabarty A.M.;
RT "Transcriptional regulation, nucleotide sequence, and localization of the
RT promoter of the catBC operon in Pseudomonas putida.";
RL J. Bacteriol. 170:1297-1304(1988).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=5330966; DOI=10.1016/s0021-9258(18)99841-8;
RA Ornston L.N.;
RT "The conversion of catechol and protocatechuate to beta-ketoadipate by
RT Pseudomonas putida. 3. Enzymes of the catechol pathway.";
RL J. Biol. Chem. 241:3795-3799(1966).
RN [4]
RP SIMILARITY TO MR.
RX PubMed=2215699; DOI=10.1038/347692a0;
RA Neidhart D.J., Kenyon G.L., Gerlt J.A., Petsko G.A.;
RT "Mandelate racemase and muconate lactonizing enzyme are mechanistically
RT distinct and structurally homologous.";
RL Nature 347:692-694(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=3612800; DOI=10.1016/0022-2836(87)90723-6;
RA Goldman A., Ollis D.L., Steitz T.A.;
RT "Crystal structure of muconate lactonizing enzyme at 3-A resolution.";
RL J. Mol. Biol. 194:143-153(1987).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RC STRAIN=PRS2000;
RX PubMed=7500361; DOI=10.1006/jmbi.1995.0666;
RA Helin S., Kahn P.C., Guha B.L., Mallows D.J., Goldman A.;
RT "The refined X-ray structure of muconate lactonizing enzyme from
RT Pseudomonas putida PRS2000 at 1.85-A resolution.";
RL J. Mol. Biol. 254:918-941(1995).
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; Evidence={ECO:0000269|PubMed:5330966};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-
CC 4,5-dihydro-2-furylacetate from catechol: step 2/3.
CC -!- SUBUNIT: Homooctamer.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000305}.
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DR EMBL; M19460; AAA25766.1; -; Genomic_DNA.
DR EMBL; M16236; AAA25765.1; -; Genomic_DNA.
DR PIR; A28630; A28630.
DR PDB; 1MUC; X-ray; 1.85 A; A/B=1-375.
DR PDB; 2MUC; X-ray; 2.30 A; A/B=1-375.
DR PDB; 3MUC; X-ray; 2.30 A; A/B=5-374.
DR PDBsum; 1MUC; -.
DR PDBsum; 2MUC; -.
DR PDBsum; 3MUC; -.
DR AlphaFoldDB; P08310; -.
DR SMR; P08310; -.
DR STRING; 1240350.AMZE01000026_gene4644; -.
DR PRIDE; P08310; -.
DR eggNOG; COG4948; Bacteria.
DR BioCyc; MetaCyc:MON-3423; -.
DR BRENDA; 5.5.1.1; 5092.
DR SABIO-RK; P08310; -.
DR UniPathway; UPA00157; UER00259.
DR EvolutionaryTrace; P08310; -.
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 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Isomerase; Manganese;
KW Metal-binding.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..375
FT /note="Muconate cycloisomerase 1"
FT /id="PRO_0000171251"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT ACT_SITE 329
FT /note="Proton donor"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 226
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT CONFLICT 33
FT /note="T -> S (in Ref. 2; AAA25766)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="S -> T (in Ref. 2; AAA25766)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="Missing (in Ref. 1; AAA25765)"
FT /evidence="ECO:0000305"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 33..43
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1MUC"
FT TURN 57..61
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 104..122
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 177..191
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:1MUC"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:1MUC"
FT HELIX 366..372
FT /evidence="ECO:0007829|PDB:1MUC"
SQ SEQUENCE 375 AA; 40510 MW; 4C8668BF6765D061 CRC64;
MTSVLIERIE AIIVHDLPTI RPPHKLAMHT MQTQTLVLIR VRCSDGVEGI GEATTIGGLA
YGYESPEGIK ANIDAHLAPA LVGLPADNIN AAMLKLDKLA KGNTFAKSGI ESALLDAQGK
RLGLPVSELL GGRVRDSLEV AWTLASGDTA RDIAEAQHML EIRRHRVFKL KIGANPLAQD
LKHVVAIKRE LGDSASVRVD VNQYWDESQA IRACQVLGDN GIDLIEQPIS RINRSGQVRL
NQRSPAPIMA DESIESVEDA FSLAADGAAS IFALKIAKNG GPRAVLRTAQ IAEAAGIALY
GGTMLEGSIG TLASAHAFLT LRQLTWGTEL FGPLLLTEEI VNEPPQYRDF QLHIPRTPGL
GLTLDEQRLA RFARR
