HPDA_CLOSL
ID HPDA_CLOSL Reviewed; 312 AA.
AC Q38HX2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=4-hydroxyphenylacetate decarboxylase activating enzyme {ECO:0000312|EMBL:ABB05048.1};
DE EC=1.97.1.- {ECO:0000305|PubMed:16878993};
DE AltName: Full=Csd-AE {ECO:0000303|PubMed:16878993};
GN Name=csdA {ECO:0000312|EMBL:ABB05048.1};
OS Clostridium scatologenes.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 25775 / DSM 757 / JCM 1414 / NCIB 8855 / VPI 5393
RC {ECO:0000312|EMBL:ABB05048.1};
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: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:16878993};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:16878993};
CC Note=Binds 2 [4Fe-4S] clusters (PubMed:16878993). One cluster is
CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC methionine (Probable). {ECO:0000269|PubMed:16878993, ECO:0000305};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16878993}.
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000255}.
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DR EMBL; DQ227741; ABB05048.1; -; Genomic_DNA.
DR RefSeq; WP_029163541.1; NZ_CP009933.1.
DR AlphaFoldDB; Q38HX2; -.
DR SMR; Q38HX2; -.
DR STRING; 1548.CSCA_5037; -.
DR OrthoDB; 1141206at2; -.
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; 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; SFLDG01118; activating_enzymes__group_2; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
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; Repeat;
KW S-adenosyl-L-methionine.
FT CHAIN 1..312
FT /note="4-hydroxyphenylacetate decarboxylase activating
FT enzyme"
FT /id="PRO_0000403687"
FT DOMAIN 16..299
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 47..79
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 80..112
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 30
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 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 36..38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 37
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 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q30W71"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q30W71"
FT BINDING 65
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q30W71"
FT BINDING 101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q30W71"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 189..191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
SQ SEQUENCE 312 AA; 36063 MW; D11D885288537D42 CRC64;
MKEKGLIFDI QSFSVHDGPG CRTSVFFIGC PLQCKWCANP ESWTKKKHIM VAENVCKWKN
GCRSCINACS HDSIKFSEDG KLKISWDTCE KCETFDCVNM CPNNALKQCV KEYTVDELMT
ILKRDFNNWG SDGGVTFTGG DPLMHHEFLV EVLKKCYDSQ IHKAIETSGY AKQEVFLEVL
KYIDFAFIDV KNMDREKHKQ GTGVYNDLIL SNIEALKKSN WNGRLVLRQP TIAGYNDSDE
NAYKLIEFMN KNSLYEINLL KFHRLGETKW NQLGKEYEYS KYGDMTNEKM EHLQQLYLDN
NIACYIGDNT PF
