MHPB_KLEP3
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 25-MAY-2022, entry version 65.
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}; OrderedLocusNames=KPK_2202;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; 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;
CC Evidence={ECO:0000255|HAMAP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000964; ACI06844.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XQJ0; -.
DR SMR; B5XQJ0; -.
DR EnsemblBacteria; ACI06844; ACI06844; KPK_2202.
DR KEGG; kpe:KPK_2202; -.
DR HOGENOM; CLU_078149_0_0_6; -.
DR OMA; MDVDHGT; -.
DR OrthoDB; 1728007at2; -.
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 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.
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