PHACB_EMEND
ID PHACB_EMEND Reviewed; 517 AA.
AC Q078T0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=3-hydroxyphenylacetate 6-hydroxylase;
DE EC=1.14.13.63 {ECO:0000269|PubMed:10329644, ECO:0000269|PubMed:17189487};
GN Name=phacB; Synonyms=pshA;
OS Emericella nidulans (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=162425;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION, AND
RP INDUCTION.
RC STRAIN=biA1;
RX PubMed=17189487; DOI=10.1128/ec.00226-06;
RA Ferrer-Sevillano F., Fernandez-Canon J.M.;
RT "Novel phacB-encoded cytochrome P450 monooxygenase from Aspergillus
RT nidulans with 3-hydroxyphenylacetate 6-hydroxylase and 3,4-
RT dihydroxyphenylacetate 6-hydroxylase activities.";
RL Eukaryot. Cell 6:514-520(2007).
RN [2]
RP CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=biA1;
RX PubMed=10329644; DOI=10.1074/jbc.274.21.14545;
RA Mingot J.M., Penalva M.A., Fernandez-Canon J.M.;
RT "Disruption of phacA, an Aspergillus nidulans gene encoding a novel
RT cytochrome P450 monooxygenase catalyzing phenylacetate 2-hydroxylation,
RT results in penicillin overproduction.";
RL J. Biol. Chem. 274:14545-14550(1999).
CC -!- FUNCTION: Catalyzes the hydroxylation of 3-hydroxyphenylacetate and
CC 3,4-dihydroxyphenylacetate to 2,5-dihydroxyphenylacetate
CC (homogentisate) and 2,4,5-trihydroxyphenylacetate, respectively. Both
CC of these compounds are used as substrate by homogentisate dioxygenase
CC in the homogentisate pathway. The homogentisate pathway is used to
CC catabolize phenylacetate and use it as a carbon source. Can also
CC catalyze the hydroxylation of phenylacetate to 2-hydroxyphenylacetate
CC at low efficiency to compensate for loss of phacA.
CC {ECO:0000269|PubMed:17189487}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxyphenylacetate + H(+) + NADH + O2 = H2O +
CC homogentisate + NAD(+); Xref=Rhea:RHEA:22208, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16169,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58149;
CC EC=1.14.13.63; Evidence={ECO:0000269|PubMed:10329644,
CC ECO:0000269|PubMed:17189487};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxyphenylacetate + H(+) + NADPH + O2 = H2O +
CC homogentisate + NADP(+); Xref=Rhea:RHEA:22204, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16169,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58149, ChEBI:CHEBI:58349;
CC EC=1.14.13.63; Evidence={ECO:0000269|PubMed:10329644,
CC ECO:0000269|PubMed:17189487};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxyphenylacetate + H(+) + NADH + O2 = 2,4,5-
CC trihydroxyphenylacetate + H2O + NAD(+); Xref=Rhea:RHEA:54088,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17612, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:138056; Evidence={ECO:0000269|PubMed:10329644,
CC ECO:0000269|PubMed:17189487};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxyphenylacetate + H(+) + NADPH + O2 = 2,4,5-
CC trihydroxyphenylacetate + H2O + NADP(+); Xref=Rhea:RHEA:54092,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17612, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:138056; Evidence={ECO:0000269|PubMed:10329644,
CC ECO:0000269|PubMed:17189487};
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC -!- INDUCTION: Induced by phenylacetate and all its monohydroxy- and
CC dihydroxy-derivatives. Induced by phenylalanine and tyrosine.
CC {ECO:0000269|PubMed:10329644, ECO:0000269|PubMed:17189487}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; DQ217596; ABB20530.1; -; Genomic_DNA.
DR AlphaFoldDB; Q078T0; -.
DR SMR; Q078T0; -.
DR BRENDA; 1.14.13.63; 517.
DR UniPathway; UPA00930; -.
DR GO; GO:0047094; F:3-hydroxyphenylacetate 6-hydroxylase activity; IMP:AspGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0010124; P:phenylacetate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Metal-binding; Monooxygenase; NAD; Oxidoreductase.
FT CHAIN 1..517
FT /note="3-hydroxyphenylacetate 6-hydroxylase"
FT /id="PRO_0000418445"
FT BINDING 449
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 517 AA; 58096 MW; EBC94FC141B6CCFD CRC64;
MAIAEALLFV NNRAVEHPLQ FLTAVAFAVP LLYVVINEFI RASARIPGFK GPRGLPLIGN
LAQIRKDAAE QYRIWSKIYG PVYQIQLGNI PVLVVNSAAA AKVLFGQNAQ ALSSRPEFYT
FHKIVSNTAG TTIGTSPYSE SLKRRRKGAA SALNRPSVES YVHHLDVESK AFVAELFKYG
NGGKTPVDPM AMIQRLSLSL ALTLNWGVRV ASQEEELFDE ITEVEDKISK FRSTTGNLQD
YIPILRLNPF SSNSHKAKEM RDRRDKYLSS LNRDLDDRME KGTHKPCIQA NVILDKEAKL
NSEELTSISL TMLSGGLDTV TTLVAWSISL LAQRPDIQDK AAKAIQEMYS EGQPLCDPAD
DQKCAYVAAL VRECLRYYTV LRLALPRTSI RDITYDGKVI PKGTVFFLNA WACNMDPEVW
SDPDEFRPER WFEQPDAPMF TYGMGYRMCA GSLLANRELY LVFIRTLNSF RIEPTEEKIE
WHPLKGNSDP TSLVAIPKKY KVRFVPKNEV SLVEALS
