MHPB2_PSEPU
ID MHPB2_PSEPU Reviewed; 314 AA.
AC Q9F9U5; Q49KF7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase 2;
DE EC=1.13.11.16;
DE AltName: Full=3-carboxyethylcatechol 2,3-dioxygenase 2;
GN Name=mhpB2; Synonyms=cbzE2;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid pHMT112, and Plasmid pKW1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ML2; PLASMID=pHMT112;
RA Panicker G., Tan H.M.;
RT "mhpB from Pseudomonas putida ML2.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GJ31; PLASMID=pKW1;
RA Reineke W., Kunze M.;
RT "GJ31 meta-operon.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX50134.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF176355; AAG09232.1; -; Genomic_DNA.
DR EMBL; AY831461; AAX50134.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q9F9U5; -.
DR SMR; Q9F9U5; -.
DR PRIDE; Q9F9U5; -.
DR UniPathway; UPA00714; -.
DR GO; GO:0047070; F:3-carboxyethylcatechol 2,3-dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Oxidoreductase;
KW Plasmid.
FT CHAIN 1..314
FT /note="2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic
FT acid 1,2-dioxygenase 2"
FT /id="PRO_0000337663"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CONFLICT 20
FT /note="N -> T (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="E -> A (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="A -> V (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 89..90
FT /note="DV -> EL (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="D -> E (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="D -> E (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="N -> D (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="R -> Q (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="N -> D (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="R -> Q (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="L -> V (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="A -> S (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="S -> A (in Ref. 1; AAX50134)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 34581 MW; F1B8670FF5D5BD50 CRC64;
MNAYLHCLSH TPLIGHFDPN QDVLDEVAEV VRAARARIEA FNPELVVLFA PDHYNGFFYD
VMPPFCLGME AEAIGDFGSL AGTLSVPKDV AEACAESVLT SGIDLAVSYR MQVDHGFAQP
LDFLLGGLDK YPVLPVFVNC VAPPLPTFER VRLLGDAIGR FTRGLNKRVL FLGSGGLSHQ
PPVPELAKVD ARMADRLMGS GRNLPPEERD ARTQRVVVAA ERFVENQNTL HPLNPKWDRY
FLDVVEQDLL SQLDDLSNAH LSELAGKSTH EVKAWVAAFS ALSAHGAYTA TDRYYRPIPE
WIAGFGSISA HTQR
