ID A3CKN0_STRSV Unreviewed; 267 AA.
AC A3CKN0;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE SubName: Full=Pyruvate formate-lyase 3, putative {ECO:0000313|EMBL:ABN43735.1};
DE EC=1.97.1.4 {ECO:0000313|EMBL:ABN43735.1};
GN OrderedLocusNames=SSA_0277 {ECO:0000313|EMBL:ABN43735.1};
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN43735.1, ECO:0000313|Proteomes:UP000002148};
RN [1] {ECO:0000313|EMBL:ABN43735.1, ECO:0000313|Proteomes:UP000002148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36 {ECO:0000313|EMBL:ABN43735.1,
RC ECO:0000313|Proteomes:UP000002148};
RX PubMed=17277061; DOI=10.1128/JB.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN43735.1; -; Genomic_DNA.
DR RefSeq; YP_001034285.1; NC_009009.1.
DR AlphaFoldDB; A3CKN0; -.
DR STRING; 388919.SSA_0277; -.
DR KEGG; ssa:SSA_0277; -.
DR PATRIC; fig|388919.9.peg.268; -.
DR eggNOG; COG1180; Bacteria.
DR HOGENOM; CLU_058969_0_0_9; -.
DR OMA; PWKYIEP; -.
DR OrthoDB; 9782387at2; -.
DR Proteomes; UP000002148; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; 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 ECO:0000313|EMBL:ABN43735.1}; Pyruvate {ECO:0000313|EMBL:ABN43735.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002148};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 26..264
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 267 AA; 30687 MW; 7ECA0A9EA2290664 CRC64;
MIVSKGGLSM ETTKGIIFNI QHFSIHDGPG IRTTVFLKGC PLRCPWCSNP ESQQFRPEPM
LDATTKKSIT MGEERSVEEI INEVLKDRDF YEESGGGLTL SGGEIFAQFE FAKAILKAAK
EKGIHTAIET TAFVEHEKFV DLIQYVDFIY TDLKHYNSVN HRKVTGVKNE LIVQNIHYAF
THQKTIVLRI PVIPDFNDSL EDAERFATLF NELSINQVQL LPFHQFGENK YKLLGRKYAM
EDVKALHPED LFEYQDVFLK HDINCYF
//