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MHPA1_BURVG
ID   MHPA1_BURVG             Reviewed;         615 AA.
AC   A4JPY1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase 1 {ECO:0000255|HAMAP-Rule:MF_01652};
DE            Short=3-HCI hydroxylase 1 {ECO:0000255|HAMAP-Rule:MF_01652};
DE            Short=3-HPP hydroxylase 1 {ECO:0000255|HAMAP-Rule:MF_01652};
DE            EC=1.14.13.127 {ECO:0000255|HAMAP-Rule:MF_01652};
GN   Name=mhpA1 {ECO:0000255|HAMAP-Rule:MF_01652};
GN   OrderedLocusNames=Bcep1808_5388;
OS   Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS   (strain R1808)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=269482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G4 / LMG 22486;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia vietnamiensis G4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000615; ABO58334.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4JPY1; -.
DR   SMR; A4JPY1; -.
DR   STRING; 269482.Bcep1808_5388; -.
DR   EnsemblBacteria; ABO58334; ABO58334; Bcep1808_5388.
DR   KEGG; bvi:Bcep1808_5388; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_009665_20_2_4; -.
DR   OMA; AHAMPPW; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000002287; 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..615
FT                   /note="3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic
FT                   acid hydroxylase 1"
FT                   /id="PRO_0000337627"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         27..56
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
FT   BINDING         294..304
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
SQ   SEQUENCE   615 AA;  67814 MW;  F54E07B75CAD7599 CRC64;
     MRPAFEPAAG LGRAHPHETT PRSIDADVAI IGAGPVGLMI ANILGLQGVR VVVVEKLTQI
     IDYPRAIGLD DEALRVFQSV GLAEALLPHT TPNHWMRFTL NGKCFASIEP RTDEFGWPRR
     NAFIQPLADQ ILYRGLERFD HVSTLLGHNV DRFAQDESGV TIDATDAHGV RTTIRAAYMV
     GADGGNSFVR RTLDVPFEGR TKPNQWIVID VRNDPIGSPH VYLHCDARRP YVSAALPHGI
     RRFEFMVMPG ETEEELSKPE NMAALVRGVV DDPDKVDYIR QRVYTHNARL ASVFRVKRIL
     LAGDAAHIMP VWQGQGYNSG IRDASNLGWK LAMVVKGTAR DALLDTYTME RRAHARSMIH
     LSEVAGDIFA PTSFVGTRVR DAFVRCFDVL PSLKRYFVEM RFKPMPRYED GVVLLARRAR
     SEGMLARLIA SRGHGAFGRL VGLMSEKRES LLGRIVHGRD AQAGTPVGRM YIQPRVRVAD
     GSIVRLDDAI GNRFAILSWG TDPTFGLTPE ARRIWSALGG CFVLAKPDPQ LGFRDDVPED
     VIAIGDVDSR LRDWFARVPE SVVLLRPDRF VAGMCSPQCV SECVSQLAQR LSLSVATGAQ
     ADDATFAPAA GLVGA
 
 
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