ID XYLE1_PSEPU Reviewed; 307 AA. AC P06622; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 27-MAR-2024, entry version 138. DE RecName: Full=Metapyrocatechase; DE Short=MPC; DE EC=1.13.11.2; DE AltName: Full=CatO2ase; DE AltName: Full=Catechol 2,3-dioxygenase; GN Name=xylE; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OG Plasmid TOL pWW0. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2; RX PubMed=6826546; DOI=10.1016/s0021-9258(18)32807-2; RA Nakai C., Kagamiyama H., Nozaki M., Nakzawa T., Inouye S., Ebina Y., RA Nakazawa A.; RT "Complete nucleotide sequence of the metapyrocatechase gene on the TOL RT plasmid of Pseudomonas putida mt-2."; RL J. Biol. Chem. 258:2923-2928(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6405380; DOI=10.1073/pnas.80.4.1101; RA Zukowski M.M., Gaffney D.F., Speck D., Kauffmann M., Findeli A., RA Wisecup A., Lecocq J.-P.; RT "Chromogenic identification of genetic regulatory signals in Bacillus RT subtilis based on expression of a cloned Pseudomonas gene."; RL Proc. Natl. Acad. Sci. U.S.A. 80:1101-1105(1983). RN [3] RP SEQUENCE REVISION. RA Zukowski M.M.; RL Submitted (MAY-1983) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1740120; DOI=10.1111/j.1432-1033.1992.tb16612.x; RA Neidle E.L., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S.; RT "Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the RT Acinetobacter calcoaceticus chromosomal benD gene are members of the short- RT chain alcohol dehydrogenase superfamily."; RL Eur. J. Biochem. 204:113-120(1992). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 284-307. RX PubMed=1791759; DOI=10.1111/j.1365-2958.1991.tb02091.x; RA Horn J.M., Harayama S., Timmis K.N.; RT "DNA sequence determination of the TOL plasmid (pWWO) xylGFJ genes of RT Pseudomonas putida: implications for the evolution of aromatic RT catabolism."; RL Mol. Microbiol. 5:2459-2474(1991). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=10368270; DOI=10.1016/s0969-2126(99)80006-9; RA Kita A., Kita S., Fujisawa I., Inaka K., Ishida T., Horiike K., Nozaki M., RA Miki K.; RT "An archetypical extradiol-cleaving catecholic dioxygenase: the crystal RT structure of catechol 2,3-dioxygenase (metapyrocatechase) from Ppseudomonas RT putida mt-2."; RL Structure 7:25-34(1999). CC -!- CATALYTIC ACTIVITY: CC Reaction=catechol + O2 = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + CC H(+); Xref=Rhea:RHEA:17337, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:18135, ChEBI:CHEBI:71198; EC=1.13.11.2; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC -!- PATHWAY: Xenobiotic degradation; toluene degradation. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family. CC {ECO:0000305}. 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; V01161; CAA24490.1; -; Genomic_DNA. DR EMBL; M64747; AAA26052.1; -; Genomic_DNA. DR PIR; A20852; A20852. DR RefSeq; NP_542866.1; NC_003350.1. DR RefSeq; WP_011005909.1; NZ_LT852425.1. DR PDB; 1MPY; X-ray; 2.80 A; A/B/C/D=1-307. DR PDBsum; 1MPY; -. DR AlphaFoldDB; P06622; -. DR SMR; P06622; -. DR BioCyc; MetaCyc:MONOMER-3421; -. DR BRENDA; 1.13.11.2; 5092. DR UniPathway; UPA00273; -. DR EvolutionaryTrace; P06622; -. DR GO; GO:0018577; F:catechol 2,3-dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro. DR GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd07243; 2_3_CTD_C; 1. DR CDD; cd07265; 2_3_CTD_N; 1. DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 2. DR InterPro; IPR017624; Catechol_2-3_dOase. DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase. DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom. DR InterPro; IPR037523; VOC. DR InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2. DR NCBIfam; TIGR03211; catechol_2_3; 1. DR PANTHER; PTHR21366; GLYOXALASE FAMILY PROTEIN; 1. DR Pfam; PF00903; Glyoxalase; 2. DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1. DR PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1. DR PROSITE; PS51819; VOC; 2. PE 1: Evidence at protein level; KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; KW Metal-binding; Oxidoreductase; Plasmid; Repeat. FT CHAIN 1..307 FT /note="Metapyrocatechase" FT /id="PRO_0000085027" FT DOMAIN 7..122 FT /note="VOC 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163" FT DOMAIN 150..269 FT /note="VOC 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163" FT BINDING 153 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 214 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 265 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT STRAND 4..16 FT /evidence="ECO:0007829|PDB:1MPY" FT HELIX 18..27 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 32..36 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 54..59 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 64..73 FT /evidence="ECO:0007829|PDB:1MPY" FT HELIX 75..88 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 116..121 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 150..159 FT /evidence="ECO:0007829|PDB:1MPY" FT HELIX 161..170 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 175..181 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 187..198 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 200..205 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 207..218 FT /evidence="ECO:0007829|PDB:1MPY" FT HELIX 222..235 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 239..245 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 252..257 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 263..268 FT /evidence="ECO:0007829|PDB:1MPY" FT STRAND 280..283 FT /evidence="ECO:0007829|PDB:1MPY" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:1MPY" FT HELIX 287..291 FT /evidence="ECO:0007829|PDB:1MPY" FT TURN 293..295 FT /evidence="ECO:0007829|PDB:1MPY" FT HELIX 300..303 FT /evidence="ECO:0007829|PDB:1MPY" SQ SEQUENCE 307 AA; 35156 MW; 80F189CF33554FAA CRC64; MNKGVMRPGH VQLRVLDMSK ALEHYVELLG LIEMDRDDQG RVYLKAWTEV DKFSLVLREA DEPGMDFMGF KVVDEDALRQ LERDLMAYGC AVEQLPAGEL NSCGRRVRFQ APSGHHFELY ADKEYTGKWG LNDVNPEAWP RDLKGMAAVR FDHALMYGDE LPATYDLFTK VLGFYLAEQV LDENGTRVAQ FLSLSTKAHD VAFIHHPEKG RLHHVSFHLE TWEDLLRAAD LISMTDTSID IGPTRHGLTH GKTIYFFDPS GNRNEVFCGG DYNYPDHKPV TWTTDQLGKA IFYHDRILNE RFMTVLT //