ID   MHPA_PARXL              Reviewed;         622 AA.
AC   Q13QI0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase {ECO:0000255|HAMAP-Rule:MF_01652};
DE            Short=3-HCI hydroxylase {ECO:0000255|HAMAP-Rule:MF_01652};
DE            Short=3-HPP hydroxylase {ECO:0000255|HAMAP-Rule:MF_01652};
DE            EC=1.14.13.127 {ECO:0000255|HAMAP-Rule:MF_01652};
GN   Name=mhpA {ECO:0000255|HAMAP-Rule:MF_01652}; OrderedLocusNames=Bxeno_B0691;
GN   ORFNames=Bxe_B2329;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the insertion of one atom of molecular oxygen into
CC       position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP)
CC       and hydroxycinnamic acid (3HCI). {ECO:0000255|HAMAP-Rule:MF_01652}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-(3-hydroxyphenyl)propanoate + H(+) + NADH + O2 = 3-(2,3-
CC         dihydroxyphenyl)propanoate + H2O + NAD(+); Xref=Rhea:RHEA:24785,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:46951, ChEBI:CHEBI:57277, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.14.13.127; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-3-(3-hydroxyphenyl)prop-2-enoate + H(+) + NADH + O2 =
CC         (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + H2O + NAD(+);
CC         Xref=Rhea:RHEA:27846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:47928, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58642; EC=1.14.13.127;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01652};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01652};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_01652}.
CC   -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01652}.
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DR   EMBL; CP000271; ABE33659.1; -; Genomic_DNA.
DR   RefSeq; WP_011491019.1; NZ_CP008762.1.
DR   AlphaFoldDB; Q13QI0; -.
DR   SMR; Q13QI0; -.
DR   STRING; 266265.Bxe_B2329; -.
DR   EnsemblBacteria; ABE33659; ABE33659; Bxe_B2329.
DR   KEGG; bxb:DR64_4661; -.
DR   KEGG; bxe:Bxe_B2329; -.
DR   PATRIC; fig|266265.5.peg.5383; -.
DR   eggNOG; COG0654; Bacteria.
DR   OMA; AHAMPPW; -.
DR   OrthoDB; 867226at2; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0008688; F:3-(3-hydroxyphenyl)propionate hydroxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0019622; P:3-(3-hydroxy)phenylpropionate catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_01652; MhpA; 1.
DR   InterPro; IPR023786; 3-HPP/3HCI_hydroxylase.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..622
FT                   /note="3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic
FT                   acid hydroxylase"
FT                   /id="PRO_0000337628"
FT   BINDING         20..49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
FT   BINDING         288..298
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
SQ   SEQUENCE   622 AA;  68723 MW;  8F9BB670C0ECA94F CRC64;
     MPASNDPVAA SRRCETVSAD VAIIGAGPVG LMIANYLGLQ GVRVVVLEKL EQIIDYPRAI
     GLDDEALRVF QSVGLADVLL PHTTPDHWMR FVTHTGHCFA SIEPRTDEFG WSRRNAFIQP
     LADRVLYEGL RRFPHVQVLF GTSVSGFTQD PAGVTIEADD EKGGRRTVRA SYMVGADGGN
     SFVRRLLDVP FEGRTKPNQW IVVDVRNDPI GSPHIYMHCD PQRPYVSAAL PHGIRRFEFM
     VMPGETEEEL SKPENMAALI RKVVADPQKV DYIRKRVYTH NARLASTFRV DRVLLAGDAA
     HIMPVWQGQG YNSGIRDASN LGWKLAMVVK QLAGDALLDT YTAERRAHAR SMIHLSEVAG
     DIFAPTSRFG IKFRDAFVRT FNVVPAMKRY FVEMRFKPMP RYETGVVLLA ERKRKHGVMA
     RVLERSGHSA PGRLLGLMSE KRESLLGRLV YGRDPSCHSP VGRMFIQPRV RTAEGSVVRL
     DDVLGSRFAI IGWGSDPTFG LSPLARETWQ RLGGCFVLAK PDNQLDFHDD VPAGVIAIGD
     VQGRLKEWFA RVPESVVLLR PDRFVAGMCT PQQVSDCIGE LALKLSLKPA EQPAVKLAVP
     ERAVAPESVA GVAAVAAVAT RA