ID   MHPB_RHOSR              Reviewed;         314 AA.
AC   Q0SJD2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase;
DE            EC=1.13.11.16;
GN   Name=mhpB; OrderedLocusNames=RHA1_ro00518;
OS   Rhodococcus sp. (strain RHA1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative
CC       cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-
CC       dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-
CC       hydroxy-6-ketononatrienedioate, respectively (By similarity).
CC   -!- CATALYTIC ACTIVITY: 3-(2,3-dihydroxyphenyl)propanoate + O(2) = 2-
CC       hydroxy-6-oxonona-2,4-diene-1,9-dioate.
CC   -!- CATALYTIC ACTIVITY: 2,3-dihydroxicinnamic acid + O(2) = 2-hydroxy-
CC       6-oxonona-2,4,7-triene-1,9-dioate.
CC   -!- COFACTOR: Fe(2+) ion (By similarity).
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropionic acid
CC       degradation.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the ligB/mhpB extradiol dioxygenase family.
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DR   EMBL; CP000431; ABG92354.1; -; Genomic_DNA.
DR   RefSeq; YP_700512.1; -.
DR   GeneID; 4218680; -.
DR   GenomeReviews; CP000431_GR; RHA1_ro00518.
DR   KEGG; rha:RHA1_ro00518; -.
DR   HOGENOM; Q0SJD2; -.
DR   OMA; Q0SJD2; PLNPEWD.
DR   BioCyc; RSP101510:RHA1_RO00518-MON; -.
DR   GO; GO:0008669; F:2,3-dihydroxy-phenylpropionate 1,2-dioxygen...; IEA:HAMAP.
DR   GO; GO:0047070; F:3-carboxyethylcatechol 2,3-dioxygenase acti...; IEA:EC.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01653; -; 1.
DR   InterPro; IPR004183; Xdiol_dOase_3B.
DR   Pfam; PF02900; LigB; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase;
KW   Iron; Oxidoreductase.
FT   CHAIN         1    314       2,3-dihydroxyphenylpropionate/2,3-
FT                                dihydroxicinnamic acid 1,2-dioxygenase.
FT                                /FTId=PRO_0000337668.
FT   ACT_SITE    115    115       Proton donor (By similarity).
FT   ACT_SITE    179    179       Proton acceptor (By similarity).
SQ   SEQUENCE   314 AA;  33844 MW;  FA31D55843964567 CRC64;
     MPVALCTMSH SPLMGRNDPA QTVIDDVDAA FENARTFIAD FAPDLIVIFA PDHYNGVYYD
     LMPPFCIGAA AQSVGDYGTE SGPLNVDRDA AYTVAREVLA SGVDVAFSER MHVDHGFAQA
     LQLLVGSITA VPTVPIFINS VAEPLGPVSR VRLLGEAVGR AAANLDKRVL FVGSGGLSHD
     PPVPQFATAP TEVKEKLIDG RNPTEAERNA REQRVIDAGR DFAAGVATIA PLNPEWDRNL
     LDVLTSGEIE QIDSWTNEWF VEQAGHSSHE VRTWIAAYAA MSAAGKYRVT STFYREIPEW
     IAGFGISTAV AVDE
//