ID MHPB_ECOLI Reviewed; 314 AA. AC P0ABR9; P54711; P77048; P77461; Q2MC76; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 16-JUN-2009, entry version 31. DE RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase; DE EC=1.13.11.16; GN Name=mhpB; OrderedLocusNames=b0348, JW0339; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=96359381; PubMed=8752345; RA Spence E.L., Kawamukai M., Sanvoisin J., Braven H., Bugg T.D.H.; RT "Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes RT eutrophus (MpcI): sequence analysis and biochemical properties of a RT third family of extradiol dioxygenases."; RL J. Bacteriol. 178:5249-5256(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12 / CS520; RX PubMed=9098055; RA Ferrandez A., Garcia J.L., Diaz E.; RT "Genetic characterization and expression in heterologous hosts of the RT 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K- RT 12."; RL J. Bacteriol. 179:2573-2581(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP PROTEIN SEQUENCE OF 1-15, SUBUNIT, FUNCTION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND COFACTOR. RX MEDLINE=94002258; PubMed=8399388; DOI=10.1016/0167-4838(93)90013-H; RA Bugg T.D.H.; RT "Overproduction, purification and properties of 2,3- RT dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli."; RL Biochim. Biophys. Acta 1202:258-264(1993). RN [7] RP MUTAGENESIS OF ASP-114; HIS-115; HIS-179 AND PRO-181, AND REACTION RP MECHANISM. RX PubMed=15491145; DOI=10.1021/bi048518t; RA Mendel S., Arndt A., Bugg T.D.H.; RT "Acid-base catalysis in the extradiol catechol dioxygenase reaction RT mechanism: site-directed mutagenesis of His-115 and His-179 in RT Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase RT (MhpB)."; RL Biochemistry 43:13390-13396(2004). CC -!- FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative CC cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3- CC dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2- CC hydroxy-6-ketononatrienedioate, respectively. CC -!- CATALYTIC ACTIVITY: 3-(2,3-dihydroxyphenyl)propanoate + O(2) = 2- CC hydroxy-6-oxonona-2,4-diene-1,9-dioate. CC -!- CATALYTIC ACTIVITY: 2,3-dihydroxicinnamic acid + O(2) = 2-hydroxy- CC 6-oxonona-2,4,7-triene-1,9-dioate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=26 uM for 2,3-dihydroxyphenylpropionic acid (at 20 degrees CC Celsius and pH 8); CC KM=36 uM for 2,3-dihydroxycinnamic acid (at 20 degrees Celsius CC and pH 8); CC KM=37 uM for methyl-2,3-dihydroxyphenylpropionate (at 20 degrees CC Celsius and pH 8); CC KM=90 uM for 3-methylcatechol (at 20 degrees Celsius and pH 8); CC KM=94 uM for 3-phenethylcatechol (at 20 degrees Celsius and pH CC 8); CC KM=154 uM for 3-propylcatechol (at 20 degrees Celsius and pH 8); CC KM=185 uM for 3-ethylcatechol (at 20 degrees Celsius and pH 8); CC KM=300 uM for 2,3-dihydroxyphenoxyacetic acid (at 20 degrees CC Celsius and pH 8); CC KM=700 uM for catechol (at 20 degrees Celsius and pH 8); CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropionic acid CC degradation. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the ligB/mhpB extradiol dioxygenase 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; D86239; BAA13053.1; -; Genomic_DNA. DR EMBL; Y09555; CAA70748.1; -; Genomic_DNA. DR EMBL; U73857; AAB18072.1; -; Genomic_DNA. DR EMBL; U00096; AAC73451.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76130.1; -; Genomic_DNA. DR PIR; D64762; D64762. DR RefSeq; AP_001000.1; -. DR RefSeq; NP_414882.1; -. DR GeneID; 945047; -. DR GenomeReviews; AP009048_GR; JW0339. DR GenomeReviews; U00096_GR; b0348. DR KEGG; ecj:JW0339; -. DR KEGG; eco:b0348; -. DR EchoBASE; EB4167; -. DR EcoGene; EG20274; mhpB. DR HOGENOM; P0ABR9; -. DR OMA; P0ABR9; PLNPEWD. DR BioCyc; EcoCyc:DHPDIOXYGEN-MON; -. DR BioCyc; MetaCyc:DHPDIOXYGEN-MON; -. DR BRENDA; 1.13.11.16; 246. DR GO; GO:0008669; F:2,3-dihydroxy-phenylpropionate 1,2-dioxygen...; IEA:HAMAP. DR GO; GO:0047070; F:3-carboxyethylcatechol 2,3-dioxygenase acti...; IEA:EC. DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01653; -; 1. DR InterPro; IPR004183; Xdiol_dOase_3B. DR Pfam; PF02900; LigB; 1. PE 1: Evidence at protein level; KW Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; KW Direct protein sequencing; Iron; Oxidoreductase. FT CHAIN 1 314 2,3-dihydroxyphenylpropionate/2,3- FT dihydroxicinnamic acid 1,2-dioxygenase. FT /FTId=PRO_0000085103. FT ACT_SITE 115 115 Proton donor. FT ACT_SITE 179 179 Proton acceptor. FT MUTAGEN 114 114 D->A: Complete loss of extradiol cleavage FT activity. FT MUTAGEN 114 114 D->N: Low level of catalytic activity, FT 600-fold lower than the wild-type enzyme. FT More than 8000-fold decrease in affinity. FT MUTAGEN 115 115 H->A: Complete loss of extradiol cleavage FT activity. FT MUTAGEN 115 115 H->Q: Complete loss of activity. FT MUTAGEN 115 115 H->Y: Complete loss of activity. FT MUTAGEN 179 179 H->A: Complete loss of activity. FT MUTAGEN 179 179 H->Q: Complete loss of activity. FT MUTAGEN 179 179 H->Y: Complete loss of activity. FT MUTAGEN 181 181 P->A: More than 2-fold decrease in FT catalytic activity and 100-fold decrease FT in affinity. FT MUTAGEN 181 181 P->H: More than 60-fold decrease in FT catalytic activity and affinity. FT CONFLICT 138 140 ING -> NKA (in Ref. 1; BAA13053). FT CONFLICT 152 152 R -> H (in Ref. 1; BAA13053). FT CONFLICT 157 157 A -> T (in Ref. 1; BAA13053). SQ SEQUENCE 314 AA; 34196 MW; E1D5A8574E5DFE05 CRC64; MHAYLHCLSH SPLVGYVDPA QEVLDEVNGV IASARERIAA FSPELVVLFA PDHYNGFFYD VMPPFCLGVG ATAIGDFGSA AGELPVPVEL AEACAHAVMK SGIDLAVSYC MQVDHGFAQP LEFLLGGLDK VPVLPVFING VATPLPGFQR TRMLGEAIGR FTSTLNKRVL FLGSGGLSHQ PPVPELAKAD AHMRDRLLGS GKDLPASERE LRQQRVISAA EKFVEDQRTL HPLNPIWDNQ FMTLLEQGRI QELDAVSNEE LSAIAGKSTH EIKTWVAAFA AISAFGNWRS EGRYYRPIPE WIAGFGSLSA RTEN //