HPDA_CLOD6
ID HPDA_CLOD6 Reviewed; 316 AA.
AC Q18CP3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=4-hydroxyphenylacetate decarboxylase activating enzyme {ECO:0000250|UniProtKB:Q84F14};
DE Short=Hpd-AE {ECO:0000250|UniProtKB:Q84F14};
DE EC=1.97.1.- {ECO:0000250|UniProtKB:Q84F14};
GN Name=hpdA {ECO:0000312|EMBL:CAJ66975.1}; OrderedLocusNames=CD630_01550;
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: Catalyzes activation of 4-hydroxyphenylacetate decarboxylase
CC under anaerobic conditions by generation of an organic free radical on
CC a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine
CC (SAM). {ECO:0000250|UniProtKB:Q46267, ECO:0000250|UniProtKB:Q84F14}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-
CC methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+)
CC + L-methionine + semiquinone [flavodoxin]; Xref=Rhea:RHEA:61976,
CC Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:14480, Rhea:RHEA-COMP:15993,
CC Rhea:RHEA-COMP:15994, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:29947, ChEBI:CHEBI:32722, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:140311;
CC Evidence={ECO:0000250|UniProtKB:Q84F14};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q84F14};
CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:Q84F14};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q84F14}.
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000255}.
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DR EMBL; AM180355; CAJ66975.1; -; Genomic_DNA.
DR RefSeq; WP_011860651.1; NZ_CP010905.2.
DR RefSeq; YP_001086624.1; NC_009089.1.
DR AlphaFoldDB; Q18CP3; -.
DR SMR; Q18CP3; -.
DR STRING; 272563.CD630_01550; -.
DR DNASU; 4914361; -.
DR EnsemblBacteria; CAJ66975; CAJ66975; CD630_01550.
DR KEGG; cdf:CD630_01550; -.
DR KEGG; pdc:CDIF630_00274; -.
DR PATRIC; fig|272563.120.peg.168; -.
DR eggNOG; COG1180; Bacteria.
DR OMA; PWKYIEP; -.
DR PhylomeDB; Q18CP3; -.
DR BioCyc; PDIF272563:G12WB-259-MON; -.
DR Proteomes; UP000001978; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR034438; 4-hPhe_decarboxylase_activase.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR040074; BssD/PflA/YjjW.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR012839; Organic_radical_activase.
DR InterPro; IPR001989; Radical_activat_CS.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30352; PTHR30352; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000371; PFL_act_enz; 1.
DR SFLD; SFLDF00279; 4-hydroxyphenylacetate_decarbo; 1.
DR SFLD; SFLDG01118; activating_enzymes__group_2; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..316
FT /note="4-hydroxyphenylacetate decarboxylase activating
FT enzyme"
FT /id="PRO_0000403683"
FT DOMAIN 20..307
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 84..115
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 34
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 40..42
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 41
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q30W71"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q30W71"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q30W71"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q30W71"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 193..195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 267
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
SQ SEQUENCE 316 AA; 35946 MW; 911B3DB1B8344624 CRC64;
MSSQKQLEGM IFDVQSFSVH DGPGCRTTVF LNGCPLSCKW CANPESWTVR PHMMFSELSC
QYENGCTVCH GKCKNGALSF NLDNKPVIDW NICKDCESFE CVNSCYYNAF KLCAKPYTVD
ELVQVIKRDS NNWRSNGGVT FSGGEPLLQH EFLHEVLLKC HEVNIHTAIE TSACVSNEVF
NKIFNDIDFA FIDIKHMDRE KHKEQTGVYN DLILENISNL ANSDWNGRLV LRVPVISGFN
DSDENISDII SFMHKNNLVE INLLPFHRLG ESKWTQLGKE YEYSDKGDVD EGHLEELQDI
FLDNGIACYV GHETAF
