MHPA_ECOHS
ID MHPA_ECOHS Reviewed; 554 AA.
AC A7ZWZ4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=EcHS_A0411;
OS Escherichia coli O9:H4 (strain HS).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(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; CP000802; ABV04798.1; -; Genomic_DNA.
DR RefSeq; WP_001007446.1; NC_009800.1.
DR AlphaFoldDB; A7ZWZ4; -.
DR SMR; A7ZWZ4; -.
DR KEGG; ecx:EcHS_A0411; -.
DR HOGENOM; CLU_009665_20_2_6; -.
DR OMA; FHSDERQ; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000001123; 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..554
FT /note="3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic
FT acid hydroxylase"
FT /id="PRO_0000337632"
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; 62184 MW; D67D408900AC5B50 CRC64;
MAIQHPDIQP AVNHSVQVAI AGAGPVGLMM ANYLGQMGID VLVVEKLDKL IDYPRAIGID
DEALRTMQSV GLVENVLPHT TPWHAMRFLT PKGRCFADIQ PMTDEFGWPR RNAFIQPQVD
AVMLEGLSRF PNVRCLFARE LEAFSQQNDE VTLHLKTAEG QRETVKAQWL 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