ID   MHPA_ECOLU              Reviewed;         554 AA.
AC   B7N8Q4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=ECUMN_0390;
OS   Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN026 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928163; CAR11605.1; -; Genomic_DNA.
DR   RefSeq; WP_001007420.1; NC_011751.1.
DR   RefSeq; YP_002411153.1; NC_011751.1.
DR   AlphaFoldDB; B7N8Q4; -.
DR   SMR; B7N8Q4; -.
DR   STRING; 585056.ECUMN_0390; -.
DR   EnsemblBacteria; CAR11605; CAR11605; ECUMN_0390.
DR   KEGG; eum:ECUMN_0390; -.
DR   PATRIC; fig|585056.7.peg.588; -.
DR   HOGENOM; CLU_009665_20_2_6; -.
DR   OMA; FHSDERQ; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000007097; 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_1000186995"
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;  62213 MW;  FCE83A5FB6A31C75 CRC64;
     MAIQHPDIQP AVNHSVQVAI AGAGPVGLMM ANYLGQMGID VLVVEKLDKL IDYPRAIGID
     DEALRTMQSV GLVDNVLPHT TPWHAMRFLT PKGRCFADIQ PMTDEFGWPR RNAFIQPQVD
     AVMLEGLSRF PNVRCLFSRE LEAFSQQDDE VTLHLKTEEG QRETVKAQWL VACDGGASFV
     RRTLNVPFEG KTAPNQWIVV DIANDPLSTP HIYLCCDPVR PYVSAALPHA VRRFEFMVMP
     GETEEQLREP QNMRKLLSKV LPNPDNVELI RQRVYTHNAR LAQRFRIDRV LLAGDAAHIM
     PVWQGQGYNS GMRDAFNLAW KLALVIQGKA RDALLDTYQQ ERRDHAKAMI DLSVTAGNVL
     APPKRWQGTL RDGVSWLLNY LPPVKRYFLE MRFKPMPQYY GGALVREGEA KHSPVGKMFI
     QPKVTLENGD VTLLDNAIGA NFAVIGWGCN PLWGMSDEQI QQWRALGTRF IQVVPEVQIH
     TAQDNHDGVL RVGDTQGRLR SWFAQHNASL VVMRPDRFVA ATAIPQTLGK TLNKLASVMT
     LTRPDADVSV EKVA