MHPA_ECODH
ID MHPA_ECODH Reviewed; 554 AA.
AC B1XBJ4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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};
GN OrderedLocusNames=ECDH10B_1359;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB02464.1; -; Genomic_DNA.
DR RefSeq; WP_001007407.1; NC_010473.1.
DR AlphaFoldDB; B1XBJ4; -.
DR SMR; B1XBJ4; -.
DR KEGG; ecd:ECDH10B_1359; -.
DR HOGENOM; CLU_009665_20_2_6; -.
DR OMA; FHSDERQ; -.
DR BioCyc; ECOL316385:ECDH10B_RS06985-MON; -.
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..554
FT /note="3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic
FT acid hydroxylase"
FT /id="PRO_1000186994"
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; 62186 MW; 1D56CB799E9F8A8E CRC64;
MAIQHPDIQP AVNHSVQVAI AGAGPVGLMM ANYLGQMGID VLVVEKLDKL IDYPRAIGID
DEALRTMQSV GLVDDVLPHT TPWHAMRFLT PKGRCFADIQ PMTDEFGWPR RNAFIQPQVD
AVMLEGVSRF PNVRCLFSRE LEAFSQQDDE VTLHLKTAEG QREIVKAQWL VACDGGASFV
RRTLNVPFEG KTAPNQWIVV DIANDPLSTP HIYLCCDPVR PYVSAALPHA VRRFEFMVMP
GETEEQLREP QNMRKLLSKV LPNPDNVELI RQRVYTHNAR LAQRFRIDRV LLAGDAAHIM
PVWQGQGYNS GMRDAFNLAW KLALVIQGKA RDALLDTYQQ ERRDHAKAMI DLSVTAGNVL
APPKRWQGTL RDGVSWLLNY LPPVKRYFLE MRFKPMPQYY GGALMREGEA KHSPVGKMFI
QPKVTLENGD VTLLDNAIGA NFAVIGWGCN PLWGMSDEQI QQWRALGTRF IQVVPEVQIH
TAQDNHDGVL RVGDTQGRLR SWFAQHNASL VVMRPDRFVA ATAIPQTLGK TLNKLASVMT
LTRPDADVSV EKVA