ID NAHH_PSEPU Reviewed; 307 AA. AC P08127; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 16-JUN-2009, entry version 71. 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=nahH; OS Pseudomonas putida. OG Plasmid NAH7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 17485 / DSM 50208 / Stanier 111 / JCM 6158 / Biotype A; RX MEDLINE=88142541; PubMed=3481421; DOI=10.1007/BF00325689; RA Harayama S., Rekik M., Wasserfallen A., Bairoch A.; RT "Evolutionary relationships between catabolic pathways for aromatics: RT conservation of gene order and nucleotide sequences of catechol RT oxidation genes of pWW0 and NAH7 plasmids."; RL Mol. Gen. Genet. 210:241-247(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 17485 / DSM 50208 / Stanier 111 / JCM 6158 / Biotype A; RX MEDLINE=87305588; PubMed=3623105; DOI=10.1016/0378-1119(87)90244-7; RA Ghosal D., You I.-S., Gunsalus I.C.; RT "Nucleotide sequence and expression of gene nahH of plasmid NAH7 and RT homology with gene xylE of TOL pWWO."; RL Gene 55:19-28(1987). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8. RC STRAIN=ATCC 17485 / DSM 50208 / Stanier 111 / JCM 6158 / Biotype A; RX MEDLINE=91129237; PubMed=1993181; DOI=10.1021/bi00220a028; RA You I.-S., Ghosal D., Gunsalus I.C.; RT "Nucleotide sequence analysis of the Pseudomonas putida PpG7 RT salicylate hydroxylase gene (nahG) and its 3'-flanking region."; RL Biochemistry 30:1635-1641(1991). CC -!- CATALYTIC ACTIVITY: Catechol + O(2) = 2-hydroxymuconate CC semialdehyde. CC -!- COFACTOR: Fe(2+) ion. CC -!- PATHWAY: Aromatic compound metabolism; benzoic acid degradation CC via hydroxylation. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M17159; AAA98183.1; -; Genomic_DNA. DR EMBL; X06412; CAA29701.1; -; Genomic_DNA. DR EMBL; M60055; AAA25899.1; -; Genomic_DNA. DR PIR; A27389; A27389. DR RefSeq; YP_534833.1; -. DR HSSP; P06622; 1MPY. DR SMR; P08127; 1-307. DR GeneID; 3974217; -. DR BRENDA; 1.13.11.2; 403. DR GO; GO:0018577; F:catechol 2,3-dioxygenase activity; IEA:EC. DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR017624; Catechol_2-3_dOase. DR InterPro; IPR004360; Glyas_bleo-R_dOase. DR InterPro; IPR000486; Xdiol_dOase_1_2. DR Pfam; PF00903; Glyoxalase; 2. DR ProDom; PD002334; Gly_diox; 2. DR TIGRFAMs; TIGR03211; catechol_2_3; 1. DR PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1. PE 3: Inferred from homology; KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding; KW Oxidoreductase; Plasmid. FT CHAIN 1 307 Metapyrocatechase. FT /FTId=PRO_0000085024. FT METAL 153 153 Iron (By similarity). FT METAL 214 214 Iron (By similarity). FT METAL 265 265 Iron (By similarity). SQ SEQUENCE 307 AA; 34913 MW; 140465CAA0CE7F4E CRC64; MNKGVMRPGH VQLRVLDMGK ALEHYVELLG LIEMDRDDQG RVYLKAWTEV DKFSVVLREA DEPGMDFMGF KVVDEDSLNR LTDDLLNFGC LIENVAAGEL KGCGRRVRFQ APSGHHFELY ADKEYTGKWG VSEVNPEAWP RDLKGMAAVR FDHCLLYGDE LQATYELFTE VLGFYLAEQV VDADGIRLAQ FLSLSTKAHD VAFIHHAEKG KFHHASFFLD TWEDVLRAAD LISMTDTSID IGPTRHGLTQ GKTIYFFDPS GNRCEVFCGG NYNYPDHKPV TWLAKDVGKA IFYHDRVLNE RFMTVMT //