HPDA_CLODR
ID HPDA_CLODR Reviewed; 316 AA.
AC C9YHW3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 65.
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:CBE01729.1}; OrderedLocusNames=CDR20291_0154;
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: 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBE01729.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FN545816; CBE01729.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_009888001.1; NC_013316.1.
DR AlphaFoldDB; C9YHW3; -.
DR SMR; C9YHW3; -.
DR PRIDE; C9YHW3; -.
DR EnsemblBacteria; CBE01729; CBE01729; CDR20291_0154.
DR KEGG; cdl:CDR20291_0154; -.
DR HOGENOM; CLU_058969_0_0_9; -.
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 S-adenosyl-L-methionine.
FT CHAIN 1..316
FT /note="4-hydroxyphenylacetate decarboxylase activating
FT enzyme"
FT /id="PRO_0000403686"
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; 36029 MW; 933F8ED5CA966724 CRC64;
MSSQKQLEGM IFDVQSFSVH DGPGCRTTVF LNGCPLSCKW CANPESWTVR PHMMFSELSC
QYENGCTVCH GKCKNGALSF NLDNKPVIDW NICKDCESFE CVNSCYYNAF KLCAKPYTVD
ELVQVIKRDS NNWRSNGGVT FSGGEPLLQH EFLHEVLLKC HEVNIHTAIE TSACVSNEVF
NKIFKDIDFA FIDIKHMDRE KHKEQTGVYN DLILENISNL ANSDWNGRLV LRVPVISGFN
DSAENISDII SFMHKNNLIE INLLPFHRLG ESKWIQLGKE YEYSDKGDID EEHLEELQDI
FLDNGIACYV GHETAF
