ID   HPAH_GEOP9              Reviewed;         494 AA.
AC   Q4L1M7;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=4-hydroxyphenylacetate 3-monooxygenase oxygenase component;
DE            EC=1.14.14.9;
DE   AltName: Full=4-HPA 3-hydroxylase;
DE   AltName: Full=4-hydroxyphenylacetate-3-hydroxylase;
GN   Name=hpaH; Synonyms=pheH;
OS   Geobacillus sp. (strain PA-9).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=278858;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=17805928; DOI=10.1007/s00284-007-9016-5;
RA   Hawumba J.F., Brozel V.S., Theron J.;
RT   "Cloning and Characterization of a 4-Hydroxyphenylacetate 3-Hydroxylase
RT   From the Thermophile Geobacillus sp. PA-9.";
RL   Curr. Microbiol. 55:480-484(2007).
CC   -!- FUNCTION: Utilizes FADH(2) supplied by HpaI, to catalyze the
CC       hydroxylation of 4-hydroxyphenylacetic acid, leading to the production
CC       of 3,4-dihydroxyphenylacetic acid (DHPA).
CC       {ECO:0000269|PubMed:17805928}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxyphenylacetate + FADH2 + O2 = 3,4-
CC         dihydroxyphenylacetate + FAD + H(+) + H2O; Xref=Rhea:RHEA:30595,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17612, ChEBI:CHEBI:48999, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307; EC=1.14.14.9;
CC   -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC       degradation; pyruvate and succinate semialdehyde from 4-
CC       hydroxyphenylacetate: step 1/7.
CC   -!- SUBUNIT: 4-HPA 3-monooxygenase consists of a reductase component HpaI
CC       and an oxygenase component HpaH.
CC   -!- SIMILARITY: Belongs to the FADH(2)-utilizing monooxygenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY549312; AAT28189.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4L1M7; -.
DR   SMR; Q4L1M7; -.
DR   BRENDA; 1.14.14.9; 7484.
DR   UniPathway; UPA00208; UER00416.
DR   GO; GO:0052881; F:4-hydroxyphenylacetate 3-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0010124; P:phenylacetate catabolic process; IEA:InterPro.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   InterPro; IPR004925; HpaB/PvcC/4-BUDH.
DR   InterPro; IPR024719; HpaB/PvcC/4-BUDH_C.
DR   InterPro; IPR024674; HpaB/PvcC/4-BUDH_N.
DR   InterPro; IPR012687; HpaB_Deino-type.
DR   PANTHER; PTHR36117; PTHR36117; 1.
DR   Pfam; PF03241; HpaB; 1.
DR   Pfam; PF11794; HpaB_N; 1.
DR   PIRSF; PIRSF000331; HpaA_HpaB; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
DR   TIGRFAMs; TIGR02309; HpaB-1; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Monooxygenase;
KW   Oxidoreductase.
FT   CHAIN           1..494
FT                   /note="4-hydroxyphenylacetate 3-monooxygenase oxygenase
FT                   component"
FT                   /id="PRO_0000387995"
FT   BINDING         103..107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149..151
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..158
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         205..206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         455..458
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  56269 MW;  47E90FE9A2E571F5 CRC64;
     MKMPAKTGKE YMERLKQAKS SVYIHGEKVE DVTVHPAFRN VVRSMAALYD RQYEKPEKML
     YRSPTTGQPV GMTFIQPTTI DELIARREAT QEWARMSAGM MGRSPDYLNA EVMAMGIAND
     LFAEDDPMFA ENAKNYYEYA REHDISLTHT LIHPQMNRAK ALHEQNDADV PLHLVERRKD
     GIIVSGIRLL ATQGGITDEI LVFPSTVKKA TSGEDPYALA FAIPNNTPGV KFICREAFDY
     GRSAWDHPLA SRFEEGDAIV SFENVFVPWE RVFVCGNSSI CNRTFRETNA VVHMSHQVVA
     KNIVKTEFLL GVTLCLIEAI GIGEFQHVKD KGAEIMLVLE TMKSHLYRAE HNAKRDRWGT
     MTPDFAALDA ARNWYPRIYP RLAEIIRILG ASGLMAIPTE ADFQHEEIGD IVRRAMQGAT
     VDGYERVQLF RLAWDLTMSA FGARQTHYEY YFFGDPVRMG MAYFDGYEKE PYKQFVREFL
     RGAKSVFIPA DNKH