ID   S6AV71_PSERE            Unreviewed;       453 AA.
AC   S6AV71;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:BAN48336.1};
DE            EC=5.5.1.2 {ECO:0000313|EMBL:BAN48336.1};
GN   Name=pcaB {ECO:0000313|EMBL:BAN48336.1};
GN   ORFNames=PCA10_26040 {ECO:0000313|EMBL:BAN48336.1};
OS   Pseudomonas resinovorans NBRC 106553.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN48336.1, ECO:0000313|Proteomes:UP000015503};
RN   [1] {ECO:0000313|EMBL:BAN48336.1, ECO:0000313|Proteomes:UP000015503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN48336.1,
RC   ECO:0000313|Proteomes:UP000015503};
RX   PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA   Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA   Fujita N., Nojiri H.;
RT   "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT   resinovorans Strain CA10 (NBRC 106553).";
RL   Genome Announc. 1:e00488-13(2013).
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       {ECO:0000256|ARBA:ARBA00034772}.
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DR   EMBL; AP013068; BAN48336.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6AV71; -.
DR   STRING; 1245471.PCA10_26040; -.
DR   KEGG; pre:PCA10_26040; -.
DR   PATRIC; fig|1245471.3.peg.2635; -.
DR   eggNOG; COG0015; Bacteria.
DR   HOGENOM; CLU_030949_3_3_6; -.
DR   OrthoDB; 9768878at2; -.
DR   Proteomes; UP000015503; Chromosome.
DR   GO; GO:0047472; F:3-carboxy-cis,cis-muconate cycloisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR   CDD; cd01597; pCLME; 1.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
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-like.
DR   NCBIfam; TIGR02426; protocat_pcaB; 1.
DR   PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43172:SF2; ADENYLOSUCCINATE LYASE C-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SMART; SM00998; ADSL_C; 1.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:BAN48336.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015503}.
FT   DOMAIN          366..445
FT                   /note="Adenylosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00998"
SQ   SEQUENCE   453 AA;  48303 MW;  B117A53C4FBC70CF CRC64;
     MNSPSNQLFD SYFTAPAMRA VFCDRGRVQG MLDFEAALAR AEANVGLVPR DAVASIVAAC
     NAELYDYAAL AQAITSAGNS AIPLVKALGK RVAAQSSEAE RYVHLGATSQ DAMDSGLVLQ
     LRAAVELLER DLAALGQALA VQAERYADTP LAGRTWLQQA TPVTLGMKLA GVLGAVTRHR
     QRLAELKPRL FCLQFGGASG SLAALGEQAW PVVEALAGEL QLNLPDQPWH TQRDRLVEFA
     SLLGLIAGSL GKLGRDLSLL MQTEAGEVFE PSAPGKGGSS TMPHKRNPVS AAVLIGAATR
     APGLVSTMFA AMPQEHERSL GLWHAEWETL PELCCLVSGA LQQALLVVPG LEVDAARMRE
     NLDLTQGLVL AEAVSIALAQ RIGRDAAHHL VEQCCRQAVK EGAHLRAVLG ANLEVTAQLS
     AAELDRLLDP AHYLGQARRW VDRALAEHQQ ISR
//