ID   MHPA_CUPPJ              Reviewed;         618 AA.
AC   Q476N1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=Reut_A0270;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ59652.1; -; Genomic_DNA.
DR   RefSeq; WP_011296460.1; NC_007347.1.
DR   AlphaFoldDB; Q476N1; -.
DR   SMR; Q476N1; -.
DR   STRING; 264198.Reut_A0270; -.
DR   EnsemblBacteria; AAZ59652; AAZ59652; Reut_A0270.
DR   KEGG; reu:Reut_A0270; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_009665_20_2_4; -.
DR   OrthoDB; 867226at2; -.
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..618
FT                   /note="3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic
FT                   acid hydroxylase"
FT                   /id="PRO_0000337642"
FT   REGION          592..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   618 AA;  68161 MW;  990BBA3A79F6BD67 CRC64;
     MNTTATQTVH ADRLPDVDTD VAIIGAGPVG LMIANILGLQ GVRVTVVEKL DQLIDYPRAI
     GLDDEALRVF QAIGLADTLL PHTTPDHWMR FVTKDGHCFA SIEPRTDEFG WSRRNAFIQP
     LADRVLFEGL QRFEHVQVLF GHGVEAFTQD GHGVSVEVTT SAGRRRTIRA AYMVGADGGN
     SIVRRALQVP FEGRTKPNQW IVVDVRNDPV GSPHIYMHCD HERPYVSAAL PHGIRRFEFM
     VMPGETEEEL SKPENMAALI RKVVADPDKV DYIRKRVYTH NARLASTFRV DRVLLAGDAA
     HIMPVWQGQG YNSGIRDANN LGWKLAMVAK GLADGRLLDT YTAERRAHAR SMIHLSEVAG
     DIFAPNTRFG VRFRDAFVRS FNVLPAVKRY FIEMRFKPMP RYEEGVVLLP PPQHRGGWLA
     RMLERAGNSA PGRLLGLMSE KRESFLGRLV YGKDPLAGSP VGRMFIQPRV RTADDRLALL
     DDAIGNGFAV IGWGTNPTFG LTPQARALAE KAGMRFVLAK PDVQLRHGDD VPDGVIAIGD
     ASGRLKEWFS RLPQSVVLLR PDRFVAGVCS PQQVSEAITE LAGKLGMTEV PPYAEASTPS
     KTSRPVLDPV TVTQAAGA