ID A0A0Q2Q950_MYCGO Unreviewed; 566 AA.
AC A0A0Q2Q950;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase {ECO:0000256|HAMAP-Rule:MF_01652};
DE Short=3-HCI hydroxylase {ECO:0000256|HAMAP-Rule:MF_01652};
DE Short=3-HPP hydroxylase {ECO:0000256|HAMAP-Rule:MF_01652};
DE EC=1.14.13.127 {ECO:0000256|HAMAP-Rule:MF_01652};
GN Name=mhpA {ECO:0000256|HAMAP-Rule:MF_01652};
GN ORFNames=AO501_27480 {ECO:0000313|EMBL:KQH76397.1};
OS Mycobacterium gordonae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH76397.1, ECO:0000313|Proteomes:UP000051677};
RN [1] {ECO:0000313|EMBL:KQH76397.1, ECO:0000313|Proteomes:UP000051677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH76397.1,
RC ECO:0000313|Proteomes:UP000051677};
RA Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA Chernousova L.;
RT "Mycobacterium gordonae draft genome assembly.";
RL Submitted (OCT-2015) 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:0000256|HAMAP-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:0000256|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:0000256|HAMAP-
CC Rule:MF_01652};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01652};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000256|HAMAP-Rule:MF_01652}.
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|HAMAP-Rule:MF_01652}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQH76397.1}.
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DR EMBL; LKTM01000350; KQH76397.1; -; Genomic_DNA.
DR RefSeq; WP_055580505.1; NZ_LKTM01000350.1.
DR AlphaFoldDB; A0A0Q2Q950; -.
DR STRING; 1778.A9W97_24850; -.
DR OrthoDB; 8670884at2; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000051677; Unassembled WGS sequence.
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; 3.30.70.2450; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 PANTHER; PTHR43476; 3-(3-HYDROXY-PHENYL)PROPIONATE/3-HYDROXYCINNAMIC ACID HYDROXYLASE; 1.
DR PANTHER; PTHR43476:SF3; FAD_BINDING_3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW ECO:0000256|HAMAP-Rule:MF_01652}; FAD {ECO:0000256|HAMAP-Rule:MF_01652};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01652};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01652};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01652};
KW Reference proteome {ECO:0000313|Proteomes:UP000051677}.
FT DOMAIN 7..342
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT BINDING 9..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01652"
FT BINDING 275..285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01652"
SQ SEQUENCE 566 AA; 61747 MW; C44CB303DAB73029 CRC64;
MTGHGTDVDV LVVGAGPVGL TLANILGLQG VRTLVAEERA TLIDYPRGVG LDDEGLRTFQ
SIGLVEQVLP HTVPNQILRF YDAKRRVLAE MAPPDAQFGW PKRNGFVQPL VDAELLRGLD
RFAHVQVRWS SPMVRCAQGG DAVRAELGGA DPVPVRARYV VGCDGGRSVT RGVMGVSFDG
TTSPTRWLVV DIAHDPLGHP NSEVGADPER PYASISIAHG IRRFEFMIHA DETDEQAEDP
AFLRRMLARM VPYPDRVEVI RRRVYTHHSR IAGNFRSGRM LLAGDAAHLM PVWQGQGYNS
GIRDAANLGW KLSAVVRGRA AEPLLDTYDV ERRKHARAMI DLSTMVGRVI SPTNRRVARA
RDAVIRSASI VPSLKRYVLE MRFKPMPRYE HGAVAHPAGV APRPGSPTGT LFIQPRVDTR
TQRDVLLDDV LGNWFAVLCW NNDPRKVLGE AAFADWKGLG ARFIALRPLT QLGWTGQDDA
DVVVVGDRGG HLKAWFDHHE ESVVFLRPDR CIAGACIAQR SAELSAALID ALSLTPRGGE
SDSATGSLLY VPQPAAESTG AAAESA
//
