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Database: UniProt
Entry: A0A1X1YS39_9MYCO
LinkDB: A0A1X1YS39_9MYCO
Original site: A0A1X1YS39_9MYCO 
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
//
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