MHPA2_BURVG
ID MHPA2_BURVG Reviewed; 546 AA.
AC A4JQH4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase 2 {ECO:0000255|HAMAP-Rule:MF_01652};
DE Short=3-HCI hydroxylase 2 {ECO:0000255|HAMAP-Rule:MF_01652};
DE Short=3-HPP hydroxylase 2 {ECO:0000255|HAMAP-Rule:MF_01652};
DE EC=1.14.13.127 {ECO:0000255|HAMAP-Rule:MF_01652};
GN Name=mhpA2 {ECO:0000255|HAMAP-Rule:MF_01652};
GN OrderedLocusNames=Bcep1808_5589;
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 3 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000616; ABO58527.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JQH4; -.
DR SMR; A4JQH4; -.
DR STRING; 269482.Bcep1808_5589; -.
DR PRIDE; A4JQH4; -.
DR EnsemblBacteria; ABO58527; ABO58527; Bcep1808_5589.
DR KEGG; bvi:Bcep1808_5589; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_20_2_4; -.
DR OMA; RRVYTHH; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000002287; Chromosome 3.
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..546
FT /note="3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic
FT acid hydroxylase 2"
FT /id="PRO_5000232604"
FT BINDING 10..39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
FT BINDING 278..288
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
SQ SEQUENCE 546 AA; 60037 MW; 899C6ABE49848E9D CRC64;
MKADNRNRTS VAIVGAGPNG AALANLLGLY GVDTVVVERA PQIVDFPRAV GIDDEALRLF
QTAGVADELS RDIIQNVPLR MFNARGECFA DVRPSVREFG WWRRNIFMQH LAERTLRDAL
ARYPHVSLRT GEEVVGLEQD DAHVTLRVQG ADGQHYALDA DYVVAADGGR SPLREMLGIP
LAGTTHPMKW VVVDVKNAGL DQPCTALNCD PRRPNVCIYL PFNYRRWEFL VFPHEDEQAI
AQPESIRALI APYVEDVERL EIVRARTYTH HSRVAERFVA GRIALVGDAA HLSPPWIGQG
LNAGLRDVGN LAWKLAGIVH GRLNPGVLAT YESERRAHAK AMIDLADTFG AMLMPTSRPV
AFLRDRLLAA ARFAPGLKDY VLQMRFKPMP SYTRGVVVTG ASDASGAIGR MIVQPDVETA
DGVRRKLDDV LGPWFSIIGW QCDPQASLSD DERAFWTALG AKFVQIVRSR SGTCREQRIA
SAHGSECVED VDNAMADWFD RHAGPLVVVR PDRYVAAQTD AVGIAGVTAA FRAFAPQQQA
EAAHVC
