ID A0A024HGS9_PSEKB Unreviewed; 452 AA.
AC A0A024HGS9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:CDF83712.1};
DE EC=5.5.1.2 {ECO:0000313|EMBL:CDF83712.1};
GN Name=pcaB {ECO:0000313|EMBL:CDF83712.1};
GN ORFNames=PKB_2365 {ECO:0000313|EMBL:CDF83712.1};
OS Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF83712.1, ECO:0000313|Proteomes:UP000025241};
RN [1] {ECO:0000313|EMBL:CDF83712.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF83712.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Linke B.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDF83712.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF83712.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W.,
RA Roy S., Van der Meer J.R.;
RT "Genome sequence of the 3-chlorobenzoate degrading bacterium Pseudomonas
RT knackmussii B13 shows multiple evidence for horizontal gene transfer.";
RL Submitted (MAY-2014) 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; HG322950; CDF83712.1; -; Genomic_DNA.
DR RefSeq; WP_043251889.1; NZ_HG322950.1.
DR AlphaFoldDB; A0A024HGS9; -.
DR STRING; 1301098.PKB_2365; -.
DR KEGG; pkc:PKB_2365; -.
DR PATRIC; fig|1301098.3.peg.2370; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_030949_3_3_6; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000025241; Chromosome.
DR GO; GO:0047472; F:3-carboxy-cis,cis-muconate cycloisomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProt.
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 Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR InterPro; IPR019468; AdenyloSucc_lyase_C.
DR InterPro; IPR024083; Fumarase/histidase_N.
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:CDF83712.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000025241}.
FT DOMAIN 366..445
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 452 AA; 48369 MW; E44D42993D484A99 CRC64;
MSTPSNRLFD AYFTQPAMRE LFCDRARLQG MLDFEAGLAR AEARAGVIPA SAVAPIEAAC
RAELYDFDAL ATAICSAGNS AIPMAKALGR QVAASDAEAE RYVHFGATSQ DAMDSGLVLQ
LRAAVGLLED DLARLATALA EQAWLHAATP MAGRTWLQHA TPVTLGMKIA GWLGAITRHR
QRLAELKPRL LSLQFGGASG SLAALGDEGF AVAEALAEEL RLQLPDQPWH TQRDRLVEFA
GWLGLVAGSL GKLGRDLSLL MQTEAGEVFE PSAPGKGGSS TMPHKRNPVA AAVLIGAATR
APGLVATMLG AMPQEHERSL GLWHAEWESL PELCCLVSGA LQQALLVVPG LEVDAERMAR
NLDLTRGLVL AEAVSIALAR RIGRDAAHHL VEQCCRQAVA ESAHLRQVLG GNAKVRAQLS
EAELDQLLDP AHYLGQCRRW VERALEEHAR LG
//
