MHPA_MYCSK
ID MHPA_MYCSK Reviewed; 573 AA.
AC A1UJP4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Mkms_3859;
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=189918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) 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: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; CP000518; ABL93052.1; -; Genomic_DNA.
DR RefSeq; WP_011561167.1; NC_008705.1.
DR AlphaFoldDB; A1UJP4; -.
DR SMR; A1UJP4; -.
DR STRING; 189918.Mkms_3859; -.
DR EnsemblBacteria; ABL93052; ABL93052; Mkms_3859.
DR KEGG; mkm:Mkms_3859; -.
DR HOGENOM; CLU_009665_20_2_11; -.
DR OMA; RRVYTHH; -.
DR OrthoDB; 867226at2; -.
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..573
FT /note="3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic
FT acid hydroxylase"
FT /id="PRO_0000337639"
FT BINDING 18..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
FT BINDING 283..293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01652"
SQ SEQUENCE 573 AA; 62570 MW; 99887CC1AFF0A10D CRC64;
MTPATARDAT ERDATDTDVV IVGAGPVGLT LANILGLQGV RTMIVEERAT LIDYPRGVGL
DDEALRTFQA IGLVDKVLPH TVPNQILRFF DGNRRLLAEM APPDARFGWP KRNGFVQPMV
DAELHAGLAR FPHVEVRWGH RMAECEETAD GVTVRLDGDP TPVRARYLVG CDGGRSATRR
LMGVSFDGTT SPTRWLVVDI ANDPLGHPNS EVGADPARPY ASISIAHGIR RFEFMIHADE
TDEQAEDPAF IHRMLGLLVP HPERVEVIRH RVYTHHSRIA GAFRKGRMFL AGDAAHLMPV
WQGQGYNSGI RDAANLGWKL AAVVDGRAGD ALLDTYDVER RKHARAMIDL STMVGRVISP
TNRRVAAVRD KLIRGASVVP TLKRYVLEMR FKPMPRYEQG AVFHPEAPSP TSPAGTLFIQ
PRVDTRDAQN VLLDEVLGTG FAVLCWNNNP RALLGADLFD RWKALGARFV AARPLTQLHW
TGHDDPDVTV IGDRTGALKG WFDAHAESVL FLRPDRCIAG ACIAQRAPEV STALFGVLHL
TQGGGNGHHG ADRPVLHVAQ SATEPSGTVA GTP
