ID   G8PKL3_PSEUV            Unreviewed;       356 AA.
AC   G8PKL3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:AEV36794.1};
DE            EC=5.5.1.2 {ECO:0000313|EMBL:AEV36794.1};
GN   Name=pcaB {ECO:0000313|EMBL:AEV36794.1};
GN   OrderedLocusNames=PSE_2284 {ECO:0000313|EMBL:AEV36794.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV36794.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT   interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV36794.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV36794.1,
RC   ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT   for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       {ECO:0000256|ARBA:ARBA00034772}.
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DR   EMBL; CP003147; AEV36794.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8PKL3; -.
DR   STRING; 911045.PSE_2284; -.
DR   KEGG; psf:PSE_2284; -.
DR   eggNOG; COG0015; Bacteria.
DR   HOGENOM; CLU_030949_3_0_5; -.
DR   Proteomes; UP000005634; Chromosome.
DR   GO; GO:0047472; F:3-carboxy-cis,cis-muconate cycloisomerase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43172:SF2; ADENYLOSUCCINATE LYASE C-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:AEV36794.1}.
FT   DOMAIN          32..294
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
SQ   SEQUENCE   356 AA;  37763 MW;  7CE161ADD5C13CD9 CRC64;
     MVVSLFTDPV WSGLFGDEEV QNAFSLKATL NHYLAYEVAL TNALSAYALI SPEAKEAVLK
     GCEGFEPDLA ALKAGVAKDG LPVPAFVAQL RAHIGEPDAA ACHKTSTSQD VMDTALALAL
     KQVSQVLTTR LAAVIDALET LKSANADHTL MGRTRMQAAL PITAGDRIVT WISPLRRYQQ
     KLEDAAKKVS ILQYGGPVGT SPIQGVHVEA IASQMAIELD LGVPTQSWHT QRDNLSDYAN
     VLSMISGSLG KLGADVALMA QQGVGEIKLT GGGSSSAMAH KHNPINAELL VTLARYNSTQ
     VSAMHSALVH EQERSGAAWA LEWMILPGMC MATGAGLQSA LKLLKQTEWI GTPLSD
//