MHPB_RHOGO
ID MHPB_RHOGO Reviewed; 314 AA.
AC O05146;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 73.
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}; Synonyms=hppB;
OS Rhodococcus globerulus.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=33008;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PWD1;
RX PubMed=9324265; DOI=10.1128/jb.179.19.6145-6153.1997;
RA Barnes M.R., Duetz W.A., Williams P.A.;
RT "A 3-(3-hydroxyphenyl)propionic acid catabolic pathway in Rhodococcus
RT globerulus PWD1: cloning and characterization of the hpp operon.";
RL J. Bacteriol. 179:6145-6153(1997).
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}.
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DR EMBL; U89712; AAB81314.1; -; Genomic_DNA.
DR RefSeq; WP_033233746.1; NZ_QEOC01000001.1.
DR AlphaFoldDB; O05146; -.
DR SMR; O05146; -.
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.
FT CHAIN 1..314
FT /note="2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic
FT acid 1,2-dioxygenase"
FT /id="PRO_0000337665"
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; 34735 MW; D6A900C8AC2F8C0A CRC64;
MKQALLCMSH SPLLHHLDPP ADVKASVEAA FDQARAFVHN FDPDVIVNFG PDHYNGFFYD
LMPPFCIGYK AKGSGDYDSF AGELNVPEAM AEDLAQFVMD QGLDIAISRQ MEVDHGAVQP
MEIIYGDVAS KPLIPVFVNS VARPFVKVAR VRKFGEAVGA YFKNSDKKVL FIGSGGLSHD
PPVPQIATAD EAQRKMLTDG RNPTPQARAA RQQRVIDTAV KFAADEADIM DLNPEWDRGF
LDVCASGRIE DFDRYTADDM DAVAGHSSHE VRNWVAAYSA LRACGEYEIA YEFYRPIKEY
ISGFAVTTAI LRDI
