ID Q88N37_PSEPK Unreviewed; 450 AA.
AC Q88N37;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:AAN67002.1};
DE EC=5.5.1.2 {ECO:0000313|EMBL:AAN67002.1};
GN Name=pcaB {ECO:0000313|EMBL:AAN67002.1};
GN OrderedLocusNames=PP_1379 {ECO:0000313|EMBL:AAN67002.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN67002.1, ECO:0000313|Proteomes:UP000000556};
RN [1] {ECO:0000313|EMBL:AAN67002.1, ECO:0000313|Proteomes:UP000000556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC {ECO:0000313|Proteomes:UP000000556};
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., Madupu R.,
RA Nelson W., White O., Peterson J., Khouri H., Hance I., Chris Lee P.,
RA Holtzapple E., Scanlan D., Tran K., Moazzez A., Utterback T., Rizzo M.,
RA Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D.,
RA Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N.,
RA Dusterhoft A., Tummler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2] {ECO:0007829|PDB:1RE5}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
RX PubMed=15301541; DOI=10.1021/bi036205c;
RA Yang J., Wang Y., Woolridge E.M., Arora V., Petsko G.A., Kozarich J.W.,
RA Ringe D.;
RT "Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from
RT Pseudomonas putida, a fumarase class II type cycloisomerase: enzyme
RT evolution in parallel pathways.";
RL Biochemistry 43:10424-10434(2004).
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC {ECO:0000256|ARBA:ARBA00034772}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015451; AAN67002.1; -; Genomic_DNA.
DR RefSeq; NP_743538.1; NC_002947.4.
DR RefSeq; WP_010952487.1; NC_002947.4.
DR PDB; 1RE5; X-ray; 2.60 A; A/B/C/D=1-450.
DR PDBsum; 1RE5; -.
DR AlphaFoldDB; Q88N37; -.
DR SMR; Q88N37; -.
DR STRING; 160488.PP_1379; -.
DR PaxDb; 160488-PP_1379; -.
DR GeneID; 83682185; -.
DR KEGG; ppu:PP_1379; -.
DR PATRIC; fig|160488.4.peg.1463; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_030949_3_3_6; -.
DR OrthoDB; 9768878at2; -.
DR PhylomeDB; Q88N37; -.
DR BioCyc; PPUT160488:G1G01-1469-MONOMER; -.
DR EvolutionaryTrace; Q88N37; -.
DR Proteomes; UP000000556; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1RE5};
KW Isomerase {ECO:0000313|EMBL:AAN67002.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000556}.
FT DOMAIN 363..442
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 450 AA; 48194 MW; 4D3F7D437C944B93 CRC64;
MSNQLFDAYF TAPAMREIFS DRGRLQGMLD FEAALARAEA SAGLVPHSAV AAIEAACQAE
RYDVGALANA IATAGNSAIP LVKALGKVIA TGVPEAERYV HLGATSQDAM DTGLVLQLRD
ALDLIEADLG KLADTLSQQA LKHADTPLVG RTWLQHATPV TLGMKLAGVL GALTRHRQRL
QELRPRLLVL QFGGASGSLA ALGSKAMPVA EALAEQLKLT LPEQPWHTQR DRLVEFASVL
GLVAGSLGKF GRDISLLMQT EAGEVFEPSA PGKGGSSTMP HKRNPVGAAV LIGAATRVPG
LLSTLFAAMP QEHERSLGLW HAEWETLPDI CCLVSGALRQ AQVIAEGMEV DAARMRRNLD
LTQGLVLAEA VSIVLAQRLG RDRAHHLLEQ CCQRAVAEQR HLRAVLGDEP QVSAELSGEE
LDRLLDPAHY LGQARVWVAR AVSEHQRFTA
//
