ID   MHPA_COMTE              Reviewed;         589 AA.
AC   Q9S158;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TA441;
RX   PubMed=10537203; DOI=10.1099/00221287-145-10-2813;
RA   Arai H., Yamamoto T., Ohishi T., Shimizu T., Nakata T., Kudo T.;
RT   "Genetic organization and characteristics of the 3-(3-
RT   hydroxyphenyl)propionic acid degradation pathway of Comamonas testosteroni
RT   TA441.";
RL   Microbiology 145:2813-2820(1999).
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; AB024335; BAA82878.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9S158; -.
DR   SMR; Q9S158; -.
DR   UniPathway; UPA00714; -.
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.
FT   CHAIN           1..589
FT                   /note="3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic
FT                   acid hydroxylase"
FT                   /id="PRO_0000337629"
FT   BINDING         15..44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
FT   BINDING         283..293
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
SQ   SEQUENCE   589 AA;  65297 MW;  7CACF905825CB744 CRC64;
     MNAPQENQAS QDDADVLIIG AGPVGLTLAN TLGMAGVRVI VAEKLPRIID YPRAIGIDDE
     SLRTLQAAGL SDQVQAHITP HHWMRFYTAS GQCFASIEPR TDEYGWSRRN AFIQPQVDDI
     LYRGLQRFDQ VQVLLGHELH SFSQDDAGIT ATLKDADGVE RTLRAKYLVA SDGGNSLVRR
     MLNVAFEGRT KPNQWIVVDV RNDPLGTPHI DMHCDPQRPY VSAALPHGIR RFEFMVMPGE
     TEEQLSRPEN LAQLMRKVVA DPDKVDYIRK RVYTHNARLA AQFRVDRILL AGDAAHIMPV
     WQGQGYNSGM RDASNLAWKL AMVVKGEARS DLLDSYEQER RDHARSMIHL SEVAGDIFAP
     ESHTAAKVRD TVMLALNAVP PVKQYFAEMR FKPMPRYEQG VVLHHTGTGN QGVRTPFAGL
     LDRSGNTPLG RLLGLMAEKK ESLVGRLVHG LETAASSPVG RMFIQPRVAT ANGHSGLLDD
     FVGLNFCILA WGTDPSYGMD EEALNFWQRL GARFIRAMPA GQLLHPTPTR DGVLTVGDEQ
     GRLKDWFSAQ GKSVVFVRPD RFVAALASPQ EVSAVTRQMA RVLHSPLEA