ID   MHPB_KLEP3              Reviewed;         314 AA.
AC   B5XQJ0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01653};
DE            EC=1.13.11.16 {ECO:0000255|HAMAP-Rule:MF_01653};
DE   AltName: Full=3-carboxyethylcatechol 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01653};
GN   Name=mhpB {ECO:0000255|HAMAP-Rule:MF_01653};
GN   OrderedLocusNames=KPK_2202;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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:0000255|HAMAP-Rule:MF_01653}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01653};
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01653};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01653};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_01653}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01653}.
CC   -!- SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01653}.
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DR   EMBL; CP000964; ACI06844.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XQJ0; -.
DR   SMR; B5XQJ0; -.
DR   KEGG; kpe:KPK_2202; -.
DR   HOGENOM; CLU_078149_0_0_6; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000001734; Chromosome.
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   Gene3D; 3.40.830.10; LigB-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.
DR   SUPFAM; SSF53213; LigB-like; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Oxidoreductase.
FT   CHAIN           1..314
FT                   /note="2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic
FT                   acid 1,2-dioxygenase"
FT                   /id="PRO_1000187009"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01653"
FT   ACT_SITE        179
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01653"
SQ   SEQUENCE   314 AA;  34295 MW;  A961455CEE055FD4 CRC64;
     MDAYLHCLSH TPLVGFVDPE QAVLDEVNGV IADARRRISA FEPELVVLFA PDHYNGFFYD
     VMPPFCLGVG ATAIGDFASA AGDLPVPTEL AEACAHAVIN SGIDLAVSYN MQVDHGFAQP
     LEFLLGGLDR VPVLPVFING VAAPLPGFQR TRLLGEAMGR FLNTLNKRVL ILGSGGLSHQ
     PPVPELAKAD AHLRDRLLGS GKQLPPDERE RRQQRVINAA RRFTEDQRSL HPLNPVWDNR
     FMSLLEQGRL AELDAIGNDE LSAMAGKSTH EIKTWVAAFA ALSAFGCWRS EGRYYRPIPE
     WIAGFGSLSA TTEI
//