ID J3JCC8_9LACO Unreviewed; 267 AA.
AC J3JCC8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Formate acetyltransferase activating enzyme {ECO:0000313|EMBL:EJN56487.1};
GN ORFNames=A11Y_46603 {ECO:0000313|EMBL:EJN56487.1};
OS Loigolactobacillus coryniformis subsp. coryniformis CECT 5711.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1185325 {ECO:0000313|EMBL:EJN56487.1, ECO:0000313|Proteomes:UP000007271};
RN [1] {ECO:0000313|EMBL:EJN56487.1, ECO:0000313|Proteomes:UP000007271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT5711 {ECO:0000313|Proteomes:UP000007271};
RA Rodriguez J.M.;
RT "Complete Genome Sequence of Lactobacillus coryniformis CECT5711.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:EJN56487.1}.
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DR EMBL; AKFP01000007; EJN56487.1; -; Genomic_DNA.
DR RefSeq; WP_004562527.1; NZ_AKFP01000007.1.
DR AlphaFoldDB; J3JCC8; -.
DR STRING; 1185325.A11Y_46603; -.
DR PATRIC; fig|1185325.3.peg.469; -.
DR Proteomes; UP000007271; Unassembled WGS sequence.
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 GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000371; PFL_act_enz; 2.
DR SFLD; SFLDG01066; organic_radical-activating_enz; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007271};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000313|EMBL:EJN56487.1}.
FT DOMAIN 23..261
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 267 AA; 29725 MW; 42E6DDD13E7BA5D2 CRC64;
MKTTQKAAPS KGLIFNIQKF SLNDGPGIRT VIFFKGCPLR CQWCANPESQ SGKPEPMYDE
QKQAPTMIGE YKTVAEIMAV ILQDRDFYAE SGGGVTFSGG EVLFQAPFAI ELAKAIHAAG
ISVICETTGY AAPAVFQEFM QQMDFMYFDC KHWSSEQHRR GTGGGNELIL KNLQTALAAR
QPLTVRIPII PQFNYTTRDA HKFGELFQRS GVTAVELLPF HQFGLKKYHE LQRDYALKGV
SQLQSADLLH YQAILAVYGV TATINGW
//
