ID   MHPA_ECOSE              Reviewed;         554 AA.
AC   B6HZX3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=ECSE_0372;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
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; AP009240; BAG75896.1; -; Genomic_DNA.
DR   RefSeq; WP_001007446.1; NC_011415.1.
DR   AlphaFoldDB; B6HZX3; -.
DR   SMR; B6HZX3; -.
DR   EnsemblBacteria; BAG75896; BAG75896; ECSE_0372.
DR   KEGG; ecy:ECSE_0372; -.
DR   HOGENOM; CLU_009665_20_2_6; -.
DR   OMA; FHSDERQ; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000008199; Chromosome.
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..554
FT                   /note="3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic
FT                   acid hydroxylase"
FT                   /id="PRO_1000186996"
FT   BINDING         17..46
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
FT   BINDING         285..295
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
SQ   SEQUENCE   554 AA;  62184 MW;  D67D408900AC5B50 CRC64;
     MAIQHPDIQP AVNHSVQVAI AGAGPVGLMM ANYLGQMGID VLVVEKLDKL IDYPRAIGID
     DEALRTMQSV GLVENVLPHT TPWHAMRFLT PKGRCFADIQ PMTDEFGWPR RNAFIQPQVD
     AVMLEGLSRF PNVRCLFARE LEAFSQQNDE VTLHLKTAEG QRETVKAQWL VACDGGASFV
     RRTLNVPFEG KTAPNQWIVV DIANDPLSTP HIYLCCDPVR PYVSAALPHA VRRFEFMVMP
     GETEEQLREP QNMRKLLSKV LPNPDNVELI RQRVYTHNAR LAQRFRIDRV LLAGDAAHIM
     PVWQGQGYNS GMRDAFNLAW KLALVIQGKA RDALLDTYQQ ERRDHAKAMI DLSVTAGNVL
     APPKRWQGTL RDGVSWLLNY LPPVKRYFLE MRFKPMPQYY GGALMREGEA KHSPVGKMFI
     QPKVTLENGD VTLLDNAIGA NFAVIGWGCN PLWGMSDEQI QQWRALGTRF IQVVPEVQIH
     TAQDNHDGVL RVGDTQGRLR SWFAQHNASL VVMRPDRFVA ATAIPQTLGK TLNKLASVMT
     LTRPDADVSV EKVA