ID A0A1X1YS39_9MYCO Unreviewed; 572 AA.
AC A0A1X1YS39;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=AWC16_03925 {ECO:0000313|EMBL:ORW13918.1};
OS Mycolicibacter longobardus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=1108812 {ECO:0000313|EMBL:ORW13918.1, ECO:0000313|Proteomes:UP000193866};
RN [1] {ECO:0000313|EMBL:ORW13918.1, ECO:0000313|Proteomes:UP000193866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45394 {ECO:0000313|EMBL:ORW13918.1,
RC ECO:0000313|Proteomes:UP000193866};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) 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:ORW13918.1}.
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DR EMBL; LQPG01000007; ORW13918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1YS39; -.
DR STRING; 1108812.AWC16_03925; -.
DR OrthoDB; 8670884at2; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000193866; 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}.
FT DOMAIN 12..350
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 551..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01652"
FT BINDING 283..293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01652"
SQ SEQUENCE 572 AA; 62406 MW; 470194CAAB01A1D4 CRC64;
MAAKKSGDGD CDVEVVVVGA GPVGLTLANI LGLQGVRTLV LEDRDTLIDY PRGVGLDDES
LRTFQAIGLV DAVLPHTVPN QILRFYDGKR RLLAEMAPAD ACFGWPKRNG FVQPLVDAEL
LRGLERFDHV RVLWGRPMTG CAETADGVTV SLGGSDGQEP QTVSARYVVG CDGGRSATRR
LMGVSFDGTT SSTRWLVIDI ANDPLGHPNS EVGADPARPY ASISIAHGIR RFEFMIHADE
TDEQAEDPEF VAAMLAPFLP RPHEVDVIRH RVYTHHSRIA GAFRRGRMLL AGDAAHLMPV
WQGQGYNSGI RDAMNLGWKL AAVVRGQARP SLLDSYDTER RKHARAMIDL STMVGKVISP
TNRRVAGIRD RVIRAASAVP TLKRYVLEMR FKPMPRYEQG AVVHDQPRRP DSPTGTLFIQ
PRVDTRTKTD LLLDDVIGTG FAVLAWNNNP RVLLGEKAFG RWAALGASFV AVRPSTQLHW
TPPDEADDPA VTIVGDRTGE LKSWFDRHSE SVLFLRPDRC IAAACIAQRA PEVSARLFDI
LALTGEGGDR PDATGPVLHV PQSTAESAGT VP
//