CATB_RHOOP
ID CATB_RHOOP Reviewed; 373 AA.
AC P95608;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 91.
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;
OS Rhodococcus opacus (Nocardia opaca).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=37919;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=1CP;
RX PubMed=8990288; DOI=10.1128/jb.179.2.370-381.1997;
RA Eulberg D., Golovleva L.A., Schloemann M.;
RT "Characterization of catechol catabolic genes from Rhodococcus erythropolis
RT 1CP.";
RL J. Bacteriol. 179:370-381(1997).
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;
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000305}.
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DR EMBL; X99622; CAA67934.1; -; Genomic_DNA.
DR RefSeq; WP_065492182.1; NZ_CP009111.1.
DR AlphaFoldDB; P95608; -.
DR SMR; P95608; -.
DR STRING; 37919.EP51_30990; -.
DR PRIDE; P95608; -.
DR GeneID; 66788846; -.
DR eggNOG; COG4948; Bacteria.
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: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..373
FT /note="Muconate cycloisomerase 1"
FT /id="PRO_0000171252"
FT ACT_SITE 169
FT /evidence="ECO:0000250"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 327
FT /note="Proton donor"
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 249
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
SQ SEQUENCE 373 AA; 39609 MW; 5EEFD786DBEEAB06 CRC64;
MTDLSIVSVE TTILDVPLVR PHKFATTSMT AQPLLLVAVT TAGGVTGYGE GVVPGGPWWG
GESVETMQAI VERYIVPVLL GRGVDEITGI MPDIERVVAN ARFAKAAVDV ALHDAWARSL
GVPVHTLLGG AFRKSVDVTW ALGAAPAEEI IEEALDLVES KRHFSFKLKM GALDPAVDTA
RVVQIAQALQ GKAGVRIDVN ARWDRLTALK YVPRLVEGGV ELIEQPTPGE QLEVLAELNR
LVPVPVMADE SVQTPHDALE VARRGAADVI ALKTTKCGGL QKSREVVAIA KAAGIACHGA
TSIEGPIGTA ASIHFACAEP GIDFGTELFG PLLFSEELLQ EPIRYADGQV FLPEGPGLGV
ELNMDAVKTW TRN
