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Database: UniProt
Entry: A0A2Y9BJK4_9FIRM
LinkDB: A0A2Y9BJK4_9FIRM
Original site: A0A2Y9BJK4_9FIRM 
ID   A0A2Y9BJK4_9FIRM        Unreviewed;       319 AA.
AC   A0A2Y9BJK4;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   28-JAN-2026, entry version 21.
DE   SubName: Full=Pyruvate formate lyase activating enzyme {ECO:0000313|EMBL:PWJ22555.1};
GN   ORFNames=A8806_11810 {ECO:0000313|EMBL:PWJ22555.1};
OS   Faecalicatena orotica.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
OC   Lachnospiraceae; Faecalicatena.
OX   NCBI_TaxID=1544 {ECO:0000313|EMBL:PWJ22555.1, ECO:0000313|Proteomes:UP000245845};
RN   [1] {ECO:0000313|EMBL:PWJ22555.1, ECO:0000313|Proteomes:UP000245845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NLAE-zl-C242 {ECO:0000313|EMBL:PWJ22555.1,
RC   ECO:0000313|Proteomes:UP000245845};
RA   Kelly W.;
RT   "The Hungate 1000. A catalogue of reference genomes from the rumen
RT   microbiome.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-
CC         methionine = glycin-2-yl radical-[protein] + semiquinone [flavodoxin]
CC         + 5'-deoxyadenosine + L-methionine + H(+); 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:ARBA00047365};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWJ22555.1}.
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DR   EMBL; QGDL01000018; PWJ22555.1; -; Genomic_DNA.
DR   RefSeq; WP_109733467.1; NZ_BAAACK010000010.1.
DR   AlphaFoldDB; A0A2Y9BJK4; -.
DR   OrthoDB; 9782387at2; -.
DR   Proteomes; UP000245845; 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; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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   InterPro; IPR058240; rSAM_sf.
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; PF00037; Fer4; 1.
DR   Pfam; PF13353; Fer4_12; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF000371; PFL_act_enz; 1.
DR   SFLD; SFLDG01118; activating_enzymes__group_2; 1.
DR   SFLD; SFLDG01066; organic_radical-activating_enz; 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; 1.
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:PWJ22555.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:PWJ22555.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245845};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          23..311
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   DOMAIN          57..86
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   319 AA;  34948 MW;  79E99356C2601EA3 CRC64;
     MVQTRINKSI EERTGLIANI ERYALNDGLG VRTTVFLKGC PLRCRWCCNP ETQKSGRELM
     FFPDTCIACG ACIESCPYGA LADSPVPDRE ICGKCADRDT TFPCVAQCYA GCRKISGERM
     TVGEVVTRAK RDMAFYLKSG GGVTVSGGEP LSQPDFLAAL LESLQANWIN TAIETCGTGK
     AEDIISIAPY VNMVFFDLKS MNDEKHKLWT GSGNRQILDN FCLMAELADK YSFELVARTP
     VIPGFNDSED EIQRIGTFIG GAKGSVAGYE LLPYHKLGRG KYQALGREYD MGETAALSDE
     KMEKLNMVAG SCGVEMCKF
//
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