ID   PCAB_PSEPU              Reviewed;         422 AA.
AC   P32427; Q59703;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 3.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=3-carboxy-cis,cis-muconate cycloisomerase;
DE            EC=5.5.1.2;
DE   AltName: Full=3-carboxymuconate lactonizing enzyme;
DE            Short=CMLE;
DE   Flags: Fragment;
GN   Name=pcaB;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
RC   STRAIN=PRS2000;
RX   PubMed=1390752; DOI=10.1021/bi00155a033;
RA   Williams S.E., Woolridge E.M., Ransom S.C., Landro J.A., Babbitt P.C.,
RA   Kozarich J.W.;
RT   "3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida is
RT   homologous to the class II fumarase family: a new reaction in the evolution
RT   of a mechanistic motif.";
RL   Biochemistry 31:9768-9776(1992).
CC   -!- FUNCTION: Catalyzes an anti cycloisomerization.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate = 3-carboxy-
CC         cis,cis-muconate + H(+); Xref=Rhea:RHEA:23656, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57496, ChEBI:CHEBI:57979; EC=5.5.1.2;
CC   -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-
CC       4,5-dihydro-2-furylacetate from 3-carboxy-cis,cis-muconate: step 1/2.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA25920.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L17082; AAA25920.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A44374; A44374.
DR   AlphaFoldDB; P32427; -.
DR   SMR; P32427; -.
DR   STRING; 1240350.AMZE01000001_gene2843; -.
DR   DrugBank; DB04447; 1,4-Dithiothreitol.
DR   DrugBank; DB04272; Citric acid.
DR   PRIDE; P32427; -.
DR   eggNOG; COG0015; Bacteria.
DR   BioCyc; MetaCyc:MON-3222; -.
DR   SABIO-RK; P32427; -.
DR   UniPathway; UPA00157; UER00265.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047472; F:3-carboxy-cis,cis-muconate cycloisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:UniProt.
DR   GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR   GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR019468; AdenyloSucc_lyase_C.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR012789; Protocat_PcaB.
DR   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SMART; SM00998; ADSL_C; 1.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR02426; protocat_pcaB; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Cytoplasm; Direct protein sequencing;
KW   Isomerase.
FT   CHAIN           1..>422
FT                   /note="3-carboxy-cis,cis-muconate cycloisomerase"
FT                   /id="PRO_0000161349"
FT   NON_TER         422
SQ   SEQUENCE   422 AA;  44676 MW;  DCB0C1E9E90DB03B CRC64;
     MTNQLFDAYF TAPAMREIFS DRGRLQGMLD FEAALARAEA AAGLVPHSAV AAIEAACKAE
     RYDVGALANA IATAGNSAIP LVKALGKVIA SGVPEAERYV HLGATSQDAM DTGLVLQLRD
     ALDLIEADLG KLADTLSQQA LKHADTPMVG RTWLQHATPV TLGMKLAGVL GALTRHRQRL
     QELGPPCWCC SSGGASGSLA ALGSKAMPVA EALAEQLKLS LPEQPWHTQR DRLVEFASVL
     GLVAGSLGKF GRDVSLLMQT EAGEVFEPSA PGKGGSSTMP HKRNPVGAAV LIGAATRVPG
     LVSTLFAAMP QEHERSLGLW HAEWETLPDI CCLVSGALRQ AQVIAEGIEV DAARMRRNLD
     LTQGLVLAEA VSIVLARTLG RDRAHHLLEQ CCQRAVAEQR HLRAVLGDDP QVSAELSAEE
     LD