HPDL_CLOD6
ID HPDL_CLOD6 Reviewed; 902 AA.
AC Q18CP5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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:CAJ66973.1}; OrderedLocusNames=CD630_01530;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ66973.1; -; Genomic_DNA.
DR RefSeq; WP_009901609.1; NZ_CP010905.2.
DR RefSeq; YP_001086622.1; NC_009089.1.
DR AlphaFoldDB; Q18CP5; -.
DR SMR; Q18CP5; -.
DR STRING; 272563.CD630_01530; -.
DR EnsemblBacteria; CAJ66973; CAJ66973; CD630_01530.
DR GeneID; 66352700; -.
DR KEGG; cdf:CD630_01530; -.
DR KEGG; pdc:CDIF630_00272; -.
DR PATRIC; fig|272563.120.peg.166; -.
DR eggNOG; COG1882; Bacteria.
DR OMA; CIDCFAS; -.
DR PhylomeDB; Q18CP5; -.
DR BioCyc; PDIF272563:G12WB-257-MON; -.
DR Proteomes; UP000001978; Chromosome.
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; Reference proteome.
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_0000403688"
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; 101294 MW; AB07DDAF3A6EB548 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 VLMNGKDYRM 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
