ID   PHACA_EMEND             Reviewed;         518 AA.
AC   Q9Y7G5; Q5AUF2;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Phenylacetate 2-hydroxylase;
DE            EC=1.14.14.54 {ECO:0000269|PubMed:10329644};
GN   Name=phacA;
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, INDUCTION,
RP   AND DISRUPTION PHENOTYPE.
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 phenylacetate to 2-
CC       hydroxyphenylacetate in the homogentisate pathway. The homogentisate
CC       pathway is used to catabolize phenylacetate and use it as a carbon
CC       source. Can also catalyze the hydroxylation of 3-hydroxyphenylacetate
CC       to 2,5-dihydroxyphenylacetate (homogentisate) at low efficiency.
CC       {ECO:0000269|PubMed:10329644}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-phenylacetate + O2 + reduced [NADPH--hemoprotein reductase]
CC         = (2-hydroxyphenyl)acetate + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:53392, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:18401, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:62423; EC=1.14.14.54;
CC         Evidence={ECO:0000269|PubMed:10329644};
CC   -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC   -!- INDUCTION: Induced by phenylacetate. {ECO:0000269|PubMed:10329644}.
CC   -!- DISRUPTION PHENOTYPE: Increases penicillin production, probably by
CC       relieving the competition for the precursor phenylacetate by the
CC       catabolic homogentisate pathway and the penicillin biosynthetic
CC       pathway. {ECO:0000269|PubMed:10329644}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AJ132442; CAB43093.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y7G5; -.
DR   SMR; Q9Y7G5; -.
DR   OMA; NYGFRIE; -.
DR   BRENDA; 1.14.14.54; 517.
DR   UniPathway; UPA00930; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0018631; F:phenylacetate hydroxylase activity; IMP:AspGD.
DR   GO; GO:0042318; P:penicillin biosynthetic process; IMP:AspGD.
DR   GO; GO:0010124; P:phenylacetate catabolic process; IMP:AspGD.
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..518
FT                   /note="Phenylacetate 2-hydroxylase"
FT                   /id="PRO_0000418444"
FT   BINDING         437
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   518 AA;  58495 MW;  9B5387AA59859A71 CRC64;
     MSLQTIGIAA VAVVYFLIRY FNRTDIPKIK GLPEVPGVPI FGNLIQLGDQ HATVAQKWAK
     KFGPVFQVRM GNKRVVFANT FDSVRQLWIK DQSALISRPT FHTFHSVVSS SQGFTIGTSP
     WDESCKRRRK AAATALNRPA TQSYMPIIDL ESMSSIRELL RDSANGTMDI NPTAYFQRFA
     LNTSLTLNYG IRIEGNVNDE LLREIVDVER GVSNFRSTSN QWQDYIPLLR IFPKMNREAE
     EFRVRRDKYL TYLLDVLKDR IAKGTDKPCI TGNILKDPEA KLNDAEIKSI CLTMVSAGLD
     TVPGNLIMGI AYLASEDGQR IQKRAHDEIM KVYPDGDAWE KCLLEEKVPY VTALVKETLR
     FWTVIPICLP RENTKDIVWN GAVIPKGTTF FMNAYAADYD ETHFTNPHAF EPERYLTASS
     DGSGTPHYGY GAGSRMCAGS HLANRELFTA YVRLITAFTM HPAKRAEDRP ILDAIECNAI
     PTALTTEPKP FKVGFKPRDP VLVRKWIAES EERTKHLN