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Entry: A0A1I0CP59_9FIRM
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Original site: A0A1I0CP59_9FIRM 
ID   A0A1I0CP59_9FIRM        Unreviewed;       306 AA.
AC   A0A1I0CP59;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Pyruvate formate lyase activating enzyme {ECO:0000313|EMBL:SET21438.1};
GN   ORFNames=SAMN04487771_100823 {ECO:0000313|EMBL:SET21438.1};
OS   [Clostridium] aminophilum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1526 {ECO:0000313|EMBL:SET21438.1, ECO:0000313|Proteomes:UP000199820};
RN   [1] {ECO:0000313|EMBL:SET21438.1, ECO:0000313|Proteomes:UP000199820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH1P1 {ECO:0000313|EMBL:SET21438.1,
RC   ECO:0000313|Proteomes:UP000199820};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000544};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC       {ECO:0000256|ARBA:ARBA00009777}.
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DR   EMBL; FOIL01000008; SET21438.1; -; Genomic_DNA.
DR   RefSeq; WP_074648924.1; NZ_FOIL01000008.1.
DR   AlphaFoldDB; A0A1I0CP59; -.
DR   STRING; 1526.SAMN02910262_00055; -.
DR   eggNOG; COG1180; Bacteria.
DR   OrthoDB; 9782387at2; -.
DR   Proteomes; UP000199820; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; 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; 3.30.70.20; -; 1.
DR   Gene3D; 3.80.30.10; pyruvate-formate lyase- activating enzyme; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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   NCBIfam; TIGR02494; PFLE_PFLC; 1.
DR   PANTHER; PTHR30352:SF4; PYRUVATE FORMATE-LYASE 2-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR   Pfam; PF13353; Fer4_12; 1.
DR   Pfam; PF14697; Fer4_21; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF000371; PFL_act_enz; 1.
DR   SFLD; SFLDG01118; activating_enzymes__group_2; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000313|EMBL:SET21438.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:SET21438.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199820};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          21..302
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   DOMAIN          52..76
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          80..109
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   306 AA;  33535 MW;  4020A9638EC931D7 CRC64;
     MDQINYELEG LVFDIQRFSV NDGPGIRTIV FLNGCPLRCQ WCSNPESQLP KTVVMFNAAE
     CIHCGRCIGT CPNGAIGKEN PAMINHDKCT GCGECTMVCP VGALILKGKR MTVAEVIEEL
     KKDSTNYRRS GGGLTVSGGE PLVQHEFTRE LLKAAHAQGW NTAIETTACA SEEVIRDVLP
     HVDLALTDVK STDSSKHEHF TGVPNTQILK GVKLVSEITK IMVRVPVIPG FNEKPEEIRQ
     IAEFAKTLNR DHLMGVNLLP YHALGENKYK MLGREYQMHG VSTLTGEEID ALKAAVEETG
     VTCRIG
//
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