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Database: UniProt
Entry: A3CKN0_STRSV
LinkDB: A3CKN0_STRSV
Original site: A3CKN0_STRSV 
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
//
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