ID   HPDL_CLODR              Reviewed;         902 AA.
AC   C9YHW1;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=4-hydroxyphenylacetate decarboxylase glycyl radical subunit {ECO:0000250|UniProtKB:Q38HX4};
DE            Short=HPA decarboxylase glycyl radical subunit {ECO:0000250|UniProtKB:Q38HX4};
DE            EC=4.1.1.83 {ECO:0000250|UniProtKB:Q38HX4};
DE   AltName: Full=4-hydroxyphenylacetate decarboxylase catalytic beta subunit {ECO:0000250|UniProtKB:Q38HX4};
DE   AltName: Full=4-hydroxyphenylacetate decarboxylase large subunit {ECO:0000250|UniProtKB:Q38HX4};
DE   AltName: Full=p-hydroxyphenylacetate decarboxylase large subunit {ECO:0000250|UniProtKB:Q38HX4};
GN   Name=hpdB {ECO:0000312|EMBL:CBE01726.1}; OrderedLocusNames=CDR20291_0152;
OS   Clostridioides difficile (strain R20291) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=645463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R20291;
RX   PubMed=19781061; DOI=10.1186/gb-2009-10-9-r102;
RA   Stabler R.A., He M., Dawson L., Martin M., Valiente E., Corton C.,
RA   Lawley T.D., Sebaihia M., Quail M.A., Rose G., Gerding D.N., Gibert M.,
RA   Popoff M.R., Parkhill J., Dougan G., Wren B.W.;
RT   "Comparative genome and phenotypic analysis of Clostridium difficile 027
RT   strains provides insight into the evolution of a hypervirulent bacterium.";
RL   Genome Biol. 10:R102.1-R102.15(2009).
CC   -!- FUNCTION: Glycyl radical subunit of the HPA decarboxylase that
CC       decarboxylates phenylacetates with a hydroxyl group in the p-position.
CC       Active toward 4-hydroxyphenylacetate and 3,4-dihydroxyphenylacetate,
CC       forming 4-methylphenol and 4-methylcatechol, respectively. Is likely
CC       involved in the catabolism of aromatic amino acids such as tyrosine
CC       fermentation. 4-methylphenol (p-cresol) formation provides metabolic
CC       toxicity, which allows an active suppression of other microbes and may
CC       provide growth advantages for the producers in highly competitive
CC       environments. The large subunit is the catalytic subunit that binds the
CC       substrate. {ECO:0000250|UniProtKB:Q38HX4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxyphenylacetate + H(+) = 4-methylphenol + CO2;
CC         Xref=Rhea:RHEA:22732, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17847, ChEBI:CHEBI:48999; EC=4.1.1.83;
CC         Evidence={ECO:0000250|UniProtKB:Q38HX4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22733;
CC         Evidence={ECO:0000250|UniProtKB:Q38HX4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,4-dihydroxyphenylacetate + H(+) = 4-methylcatechol + CO2;
CC         Xref=Rhea:RHEA:62556, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17254, ChEBI:CHEBI:17612; EC=4.1.1.83;
CC         Evidence={ECO:0000250|UniProtKB:Q38HX4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62557;
CC         Evidence={ECO:0000250|UniProtKB:Q38HX4};
CC   -!- SUBUNIT: Heterooctamer consisting of 4 large (HpdB) subunits and 4
CC       small (HpdC) subunits, arranged as a tetramer of heterodimers. Also
CC       forms a catalytically inactive homodimer.
CC       {ECO:0000250|UniProtKB:Q38HX4}.
CC   -!- PTM: Requires the activating protein CsdA to generate the key active
CC       site glycyl radical that is involved in catalysis.
CC       {ECO:0000250|UniProtKB:Q38HX4}.
CC   -!- PTM: Phosphorylated on serine. Phosphorylation may trigger the
CC       formation of the active heterooctamers and thereby regulates enzyme
CC       activity. {ECO:0000250|UniProtKB:Q38HX4}.
CC   -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. HPAD
CC       subfamily. {ECO:0000305}.
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DR   EMBL; FN545816; CBE01726.1; -; Genomic_DNA.
DR   RefSeq; WP_009892575.1; NC_013316.1.
DR   AlphaFoldDB; C9YHW1; -.
DR   SMR; C9YHW1; -.
DR   EnsemblBacteria; CBE01726; CBE01726; CDR20291_0152.
DR   KEGG; cdl:CDR20291_0152; -.
DR   HOGENOM; CLU_009096_0_1_9; -.
DR   OMA; CIDCFAS; -.
DR   GO; GO:0043722; F:4-hydroxyphenylacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001150; Gly_radical.
DR   InterPro; IPR004184; PFL_dom.
DR   Pfam; PF01228; Gly_radical; 1.
DR   Pfam; PF02901; PFL-like; 1.
DR   PROSITE; PS51149; GLY_RADICAL_2; 1.
DR   PROSITE; PS51554; PFL; 1.
PE   3: Inferred from homology;
KW   Lyase; Organic radical; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q84F16"
FT   CHAIN           2..902
FT                   /note="4-hydroxyphenylacetate decarboxylase glycyl radical
FT                   subunit"
FT                   /evidence="ECO:0000250|UniProtKB:Q84F16"
FT                   /id="PRO_0000403690"
FT   DOMAIN          38..774
FT                   /note="PFL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT   DOMAIN          782..902
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT   ACT_SITE        507
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX4"
FT   ACT_SITE        509
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX4"
FT   BINDING         348
FT                   /ligand="4-hydroxyphenylacetate"
FT                   /ligand_id="ChEBI:CHEBI:48999"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX4"
FT   BINDING         507
FT                   /ligand="4-hydroxyphenylacetate"
FT                   /ligand_id="ChEBI:CHEBI:48999"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX4"
FT   BINDING         540
FT                   /ligand="4-hydroxyphenylacetate"
FT                   /ligand_id="ChEBI:CHEBI:48999"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX4"
FT   BINDING         641
FT                   /ligand="4-hydroxyphenylacetate"
FT                   /ligand_id="ChEBI:CHEBI:48999"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX4"
FT   MOD_RES         877
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   902 AA;  101268 MW;  5AADCC0E242F5E06 CRC64;
     MSQSKEDKIR SILEAKNIKS NFQNKENLSE FNEKKASKRA EDLLDVYYNT LSTADMEFPY
     WYNREYRKSD GDIPVVRRAK ALKAAFSHMT PNIIPGEKIV MQKTRHYRGS FPMPWVSESF
     FVAQGEQMRE EAKKLASNTA DELTKFGSGG GNVTESFGNV VSIAGKFGMR KEEVPVLVKM
     AKEWVGKSVE DLGFHYEKMM PDYDLKENLM STLICMFDSG YTLPQGREVI NYFYPLNYGL
     DGIIEMAKEC KKAVAGNASG DGLIGMDRLY FYEAVIQVIE GLQTWILNYA KHAKYLESIE
     TDLEAKKEYS DLVEILEHIA HKQPRTFREA LQLTYTIHIA SVNEDAISGM SIGRFGQILY
     PWYEQDIEKG LITKEEVIEL LELYRIKITC IDCFASAGVN GGVLSGNTFN TLSIGGLKED
     GSTGANELEE LLLEASMRCR TPQPSLTMLY DEKLPEDFLM KAAECTKLGS GYPAWVNNSN
     GTTFMMKQFA DEGMTVEEAR AFALGGCLET SPGCWKQLTL NGKTYSIAGG AGQSAGSGVH
     FIANPKILEL VLMNGKDHRM NIQVFEPHNK PLDTYEEVIE VFKDYYKQAI NVLERANNIE
     LDIWRKFDTS IINSLLKPDC LDKGQHIGNM GYRYNATLNV ETCGTVTMVN SFAALKKLVY
     DDKAFTIEEM KDAILNNFGF KDALEVGNYS MADQVKVDKT GKYDAIYKAC LDAPKYGNND
     LYADNILKNY EVWLSKVCEE AQSLYAKKMY PCQISVSTHG PQGAATLATP DGRLSGTTYS
     DGSVSAYAGT DKNGVYALFE SATIWDQAVV QNSQMNLKLH PTTIKGQQGT KKLLDLTRSY
     LRKGGFHIQY NVVDSETLKD AQKNPDNYRQ LMVRVAGFTQ YWCELGKPIQ DEVIARTEYE
     GV