HPDA_CLODI
ID HPDA_CLODI Reviewed; 316 AA.
AC Q84F14;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=4-hydroxyphenylacetate decarboxylase activating enzyme {ECO:0000303|PubMed:16878993};
DE Short=Hpd-AE {ECO:0000303|PubMed:16878993};
DE EC=1.97.1.- {ECO:0000305|PubMed:15153112, ECO:0000305|PubMed:16878993};
GN Name=hpdA {ECO:0000312|EMBL:CAD65891.1};
OS Clostridioides difficile (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=1496;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 9689 / DSM 1296 / BCRC 10642 / JCM 1296 / NCIMB 10666 / NCTC
RC 11209 / 90556-M6S {ECO:0000312|EMBL:CAD65891.1};
RX PubMed=15153112; DOI=10.1111/j.1432-1033.2004.04152.x;
RA Andrei P.I., Pierik A.J., Zauner S., Andrei-Selmer L.C., Selmer T.;
RT "Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate
RT decarboxylase. A small subunit, HpdC, is essential for catalytic
RT activity.";
RL Eur. J. Biochem. 271:2225-2230(2004).
RN [2]
RP FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 9689 / DSM 1296 / BCRC 10642 / JCM 1296 / NCIMB 10666 / NCTC
RC 11209 / 90556-M6S {ECO:0000269|PubMed:16878993};
RX PubMed=16878993; DOI=10.1021/bi060840b;
RA Yu L., Blaser M., Andrei P.I., Pierik A.J., Selmer T.;
RT "4-Hydroxyphenylacetate decarboxylases: properties of a novel subclass of
RT glycyl radical enzyme systems.";
RL Biochemistry 45:9584-9592(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:0000269|PubMed:15153112,
CC ECO:0000269|PubMed:16878993}.
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:0000305|PubMed:15153112, ECO:0000305|PubMed:16878993};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:15153112, ECO:0000269|PubMed:16878993};
CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine (Probable).
CC {ECO:0000269|PubMed:15153112, ECO:0000269|PubMed:16878993,
CC ECO:0000305};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15153112,
CC ECO:0000269|PubMed:16878993}.
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000255}.
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DR EMBL; AJ543427; CAD65891.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84F14; -.
DR SMR; Q84F14; -.
DR BRENDA; 4.1.1.83; 1473.
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 SFLD; SFLDS00029; Radical_SAM; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
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_0000403685"
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; 35902 MW; 58D15C47682AB7C3 CRC64;
MSSQKQLEGM IFDVQSFSVH DGPGCRTTVF LNGCPLSCKW CANPESWTVR PHMMFSELSC
QYENGCTVCH GKCKNGALSF NLDNKPVIDW NICKDCESFE CVNSCYYNAF KLCAKPYTVD
ELVQVIKRDS NNWRSNGGVT FSGGEPLLQH EFLHEVLLKC HEVNVHTAIE TSACVSNEVF
NKIFNDIDFA FIDIKHMDRE KHKEQTGVYN DLILENISNL ANSDWNGRLV LRVPVISGFN
DSDENISDII SFMHKNNLVE INLLPFHRLG ESKWTQLGKE YEYSDKGDVD EGHLEELQDI
FLDNGIACYV GHVTAF
