ID C3KAN8_PSEFS Unreviewed; 454 AA.
AC C3KAN8;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:CAI2795662.1, ECO:0000313|EMBL:CAY47623.1};
DE EC=5.5.1.2 {ECO:0000313|EMBL:CAI2795662.1, ECO:0000313|EMBL:CAY47623.1};
GN Name=pcaB {ECO:0000313|EMBL:CAY47623.1};
GN OrderedLocusNames=PFLU_1369 {ECO:0000313|EMBL:CAY47623.1};
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY47623.1};
RN [1] {ECO:0000313|EMBL:CAY47623.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAY47623.1};
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
RN [2] {ECO:0000313|EMBL:CAI2795662.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAI2795662.1};
RA Fortmann-Grote C.;
RL Submitted (OCT-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC {ECO:0000256|ARBA:ARBA00034772}.
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DR EMBL; OV986001; CAI2795662.1; -; Genomic_DNA.
DR EMBL; AM181176; CAY47623.1; -; Genomic_DNA.
DR RefSeq; WP_012722674.1; NC_012660.1.
DR AlphaFoldDB; C3KAN8; -.
DR STRING; 294.SRM1_01288; -.
DR PATRIC; fig|216595.4.peg.1599; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_030949_3_3_6; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP001152918; 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:CAY47623.1}.
FT DOMAIN 367..446
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 454 AA; 48259 MW; B582390B5C4119AD CRC64;
MTLRTSNQLF DAYFTAGSMA EVFCDQGRLQ GMLDFEAGLA RAQAQVGLIP QAAVAPIAQA
CLASLYDVDA LGVAIATAGN SAIPLVKALG KLIASEDAGA ERYVHLGATS QDVMDTGLVL
QLRRAVALIE ADLAHLGDIL AAQAQRYAGV PLAGRTWLQH ATPVTLGMKI AGWLGAVTRS
RQRLAELKPR LLVLQFGGAS GTLAALGEQA MPVAEALAAE LQLNLPEQPW HTQRDRLVEF
ASVLGLIAGS LGKLGRDISL LMQTEAAEVF EPSAPGKGGS STMPHKRNPV GAAVLISTAT
RVPGLVSTMF SAMPQEHERS LGLWHAEWET LPEICRLVSG ALQQALLVSE GLEVDPQRMA
QNLDLTQGLV LAEAVSIVLA QRLGRETAHH LLEQCCKRAV ADGRHLRAVL ADEPQVTAEL
SAAELDRLLD PAHYLGQAHT WVTRAVTEHF ALTA
//
