MHPB_ECOLI
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 03-AUG-2022, entry version 110.
DE RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase;
DE EC=1.13.11.16 {ECO:0000269|PubMed:8399388, ECO:0000269|PubMed:8752345};
DE AltName: Full=3-carboxyethylcatechol 2,3-dioxygenase;
GN Name=mhpB; OrderedLocusNames=b0348, JW0339;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC
RP ACTIVITY, AND FUNCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8752345; DOI=10.1128/jb.178.17.5249-5256.1996;
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 third
RT 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; DOI=10.1128/jb.179.8.2573-2581.1997;
RA Ferrandez A., Garcia J.L., Diaz E.;
RT "Genetic characterization and expression in heterologous hosts of the 3-(3-
RT hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-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 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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-15, SUBUNIT, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND CATALYTIC ACTIVITY.
RX 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 Escherichia
RT coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB).";
RL Biochemistry 43:13390-13396(2004).
CC -!- FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative cleavage
CC of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid
CC into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-
CC ketononatrienedioate, respectively. {ECO:0000269|PubMed:8399388,
CC ECO:0000269|PubMed:8752345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-
CC oxonona-2,4-dienedioate + H(+); Xref=Rhea:RHEA:23840,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:46951,
CC ChEBI:CHEBI:66887; EC=1.13.11.16;
CC Evidence={ECO:0000269|PubMed:8399388, ECO:0000269|PubMed:8752345};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-
CC hydroxy-6-oxonona-2,4,7-trienedioate + H(+); Xref=Rhea:RHEA:25054,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:58642,
CC ChEBI:CHEBI:66888; EC=1.13.11.16;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26 uM for 2,3-dihydroxyphenylpropionic acid (at 20 degrees Celsius
CC and pH 8) {ECO:0000269|PubMed:8399388, ECO:0000269|PubMed:8752345};
CC KM=36 uM for 2,3-dihydroxycinnamic acid (at 20 degrees Celsius and pH
CC 8) {ECO:0000269|PubMed:8752345};
CC KM=37 uM for methyl-2,3-dihydroxyphenylpropionate (at 20 degrees
CC Celsius and pH 8) {ECO:0000269|PubMed:8752345};
CC KM=90 uM for 3-methylcatechol (at 20 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:8399388, ECO:0000269|PubMed:8752345};
CC KM=94 uM for 3-phenethylcatechol (at 20 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:8752345};
CC KM=154 uM for 3-propylcatechol (at 20 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:8752345};
CC KM=185 uM for 3-ethylcatechol (at 20 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:8752345};
CC KM=300 uM for 2,3-dihydroxyphenoxyacetic acid (at 20 degrees Celsius
CC and pH 8) {ECO:0000269|PubMed:8752345};
CC KM=700 uM for catechol (at 20 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:8752345};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8399388}.
CC -!- SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family.
CC {ECO:0000305}.
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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; NP_414882.1; NC_000913.3.
DR RefSeq; WP_000543457.1; NZ_SSZK01000061.1.
DR AlphaFoldDB; P0ABR9; -.
DR SMR; P0ABR9; -.
DR BioGRID; 4260730; 12.
DR BioGRID; 849436; 6.
DR DIP; DIP-10206N; -.
DR IntAct; P0ABR9; 12.
DR STRING; 511145.b0348; -.
DR SwissLipids; SLP:000001889; -.
DR PaxDb; P0ABR9; -.
DR PRIDE; P0ABR9; -.
DR EnsemblBacteria; AAC73451; AAC73451; b0348.
DR EnsemblBacteria; BAE76130; BAE76130; BAE76130.
DR GeneID; 945047; -.
DR KEGG; ecj:JW0339; -.
DR KEGG; eco:b0348; -.
DR PATRIC; fig|1411691.4.peg.1930; -.
DR EchoBASE; EB4167; -.
DR eggNOG; COG3384; Bacteria.
DR HOGENOM; CLU_078149_0_0_6; -.
DR InParanoid; P0ABR9; -.
DR OMA; MDVDHGT; -.
DR PhylomeDB; P0ABR9; -.
DR BioCyc; EcoCyc:DHPDIOXYGEN-MON; -.
DR BioCyc; MetaCyc:DHPDIOXYGEN-MON; -.
DR BRENDA; 1.13.11.16; 2026.
DR SABIO-RK; P0ABR9; -.
DR UniPathway; UPA00714; -.
DR PRO; PR:P0ABR9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0047070; F:3-carboxyethylcatechol 2,3-dioxygenase activity; IDA:EcoCyc.
DR GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR GO; GO:0019622; P:3-(3-hydroxy)phenylpropionate catabolic process; IMP:EcoCyc.
DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046271; P:phenylpropanoid catabolic process; IMP:EcoCyc.
DR CDD; cd07365; MhpB_like; 1.
DR HAMAP; MF_01653; MhpB; 1.
DR InterPro; IPR023789; DHPP/DHXA_dioxygenase.
DR InterPro; IPR004183; Xdiol_dOase_suB.
DR Pfam; PF02900; LigB; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW Iron; Oxidoreductase; Reference proteome.
FT CHAIN 1..314
FT /note="2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic
FT acid 1,2-dioxygenase"
FT /id="PRO_0000085103"
FT ACT_SITE 115
FT /note="Proton donor"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT MUTAGEN 114
FT /note="D->A: Complete loss of extradiol cleavage activity."
FT /evidence="ECO:0000269|PubMed:15491145"
FT MUTAGEN 114
FT /note="D->N: Low level of catalytic activity, 600-fold
FT lower than the wild-type enzyme. More than 8000-fold
FT decrease in affinity."
FT /evidence="ECO:0000269|PubMed:15491145"
FT MUTAGEN 115
FT /note="H->A: Complete loss of extradiol cleavage activity."
FT /evidence="ECO:0000269|PubMed:15491145"
FT MUTAGEN 115
FT /note="H->Q: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:15491145"
FT MUTAGEN 115
FT /note="H->Y: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:15491145"
FT MUTAGEN 179
FT /note="H->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:15491145"
FT MUTAGEN 179
FT /note="H->Q: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:15491145"
FT MUTAGEN 179
FT /note="H->Y: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:15491145"
FT MUTAGEN 181
FT /note="P->A: More than 2-fold decrease in catalytic
FT activity and 100-fold decrease in affinity."
FT /evidence="ECO:0000269|PubMed:15491145"
FT MUTAGEN 181
FT /note="P->H: More than 60-fold decrease in catalytic
FT activity and affinity."
FT /evidence="ECO:0000269|PubMed:15491145"
FT CONFLICT 138..140
FT /note="ING -> NKA (in Ref. 1; BAA13053)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="R -> H (in Ref. 1; BAA13053)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="A -> T (in Ref. 1; BAA13053)"
FT /evidence="ECO:0000305"
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
