XYLE1_PSEPU
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 03-AUG-2022, entry version 132.
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; Proteobacteria; 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}.
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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_QWEF01000005.1.
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:MON-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 Gene3D; 3.10.180.10; -; 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 Pfam; PF00903; Glyoxalase; 2.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR03211; catechol_2_3; 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
