MHPA_MYCA1
ID MHPA_MYCA1 Reviewed; 580 AA.
AC A0QB57;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=MAV_0878;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) 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; CP000479; ABK68919.1; -; Genomic_DNA.
DR RefSeq; WP_011723822.1; NC_008595.1.
DR AlphaFoldDB; A0QB57; -.
DR SMR; A0QB57; -.
DR EnsemblBacteria; ABK68919; ABK68919; MAV_0878.
DR KEGG; mav:MAV_0878; -.
DR HOGENOM; CLU_009665_20_2_11; -.
DR OMA; RRVYTHH; -.
DR OrthoDB; 867226at2; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000001574; 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..580
FT /note="3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic
FT acid hydroxylase"
FT /id="PRO_0000337634"
FT BINDING 14..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
FT BINDING 291..301
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
SQ SEQUENCE 580 AA; 63287 MW; 7EF1D63CF47DF2A3 CRC64;
MIAPGPRATD HDTDVLVVGA GPVGLTLANI LGLQGIRTVV VEERDTLIDY PRGVGLDDEA
LRTFQSIGLV ERVLPHTVPN QILRFMDAKR RVLAEMAPPD ARFGWPKRNG FVQPLVDAEL
LAGLDRFAHV QVRWGSPMTG CREDADGVNV ELGADGGNVG DGGGDGHPAG LRARYVVGCD
GGRSMTRRVM GVSFDGTTSS TRWLVVDIAN DPLGHPNSEV GADPERPYAS ISIAHGIRRF
EFMIHADESD EQAEDPEFLT RMLARMVPHP DRVDVIRRRV YTHHSRIAGE FRRGRLLLAG
DAAHLMPVWQ GQGYNSGIRD AANLGWKLAA VVSGRAGDKL LDTYDMERRK HARAMIDLST
MVGRVISPTN RRVAGARDLL VRSASIVPTL KRYVLEMRFK PMPRYEHGAV VHANPGRADS
PVGTLFIQPR VDTRDQQDVL LDDVLGPWFA VLCWNNNPRK ILGETAFANW KALGARFFAL
RPATQLRWTG HDDPDVVVVG DRRGDLKSWF DIHAESVLFL RPDRCIAGAC IAQRAPDLSA
ALFDALTLTP RGGDPQSGTG SVLYVAQPAP ESSGAVAGPA
