ID PFLA_STAAS Reviewed; 251 AA. AC Q6GCP9; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 107. DE RecName: Full=Pyruvate formate-lyase-activating enzyme; DE Short=PFL-activating enzyme; DE EC=1.97.1.4; GN Name=pflA; OrderedLocusNames=SAS0202; OS Staphylococcus aureus (strain MSSA476). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=282459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSSA476; RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence RT for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). CC -!- FUNCTION: Activation of pyruvate formate-lyase under anaerobic CC conditions by generation of an organic free radical, using S- CC adenosylmethionine and reduced flavodoxin as cosubstrates to produce CC 5'-deoxy-adenosine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=glycyl-[formate C-acetyltransferase] + reduced [flavodoxin] + CC S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical- CC [formate C-acetyltransferase] + H(+) + L-methionine + semiquinone CC [flavodoxin]; Xref=Rhea:RHEA:19225, Rhea:RHEA-COMP:10622, Rhea:RHEA- CC COMP:12190, Rhea:RHEA-COMP:12191, Rhea:RHEA-COMP:14480, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29947, CC ChEBI:CHEBI:32722, ChEBI:CHEBI:57618, ChEBI:CHEBI:57844, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:140311; EC=1.97.1.4; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX571857; CAG41970.1; -; Genomic_DNA. DR RefSeq; WP_000911657.1; NC_002953.3. DR AlphaFoldDB; Q6GCP9; -. DR SMR; Q6GCP9; -. DR KEGG; sas:SAS0202; -. DR HOGENOM; CLU_058969_1_1_9; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 GO; GO:0006006; P:glucose metabolic process; 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; IPR040074; BssD/PflA/YjjW. DR InterPro; IPR034457; Organic_radical-activating. DR InterPro; IPR012839; Organic_radical_activase. DR InterPro; IPR012838; PFL1_activating. DR InterPro; IPR034465; Pyruvate_for-lyase_activase. DR InterPro; IPR001989; Radical_activat_CS. DR InterPro; IPR007197; rSAM. DR NCBIfam; TIGR02493; PFLA; 1. DR PANTHER; PTHR30352:SF23; PYRUVATE FORMATE-LYASE 1-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; 1. DR SFLD; SFLDG01118; activating_enzymes__group_2; 1. DR SFLD; SFLDF00278; pyruvate_formate-lyase_activas; 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; Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Iron; KW Iron-sulfur; Metal-binding; Oxidoreductase; S-adenosyl-L-methionine. FT CHAIN 1..251 FT /note="Pyruvate formate-lyase-activating enzyme" FT /id="PRO_0000271715" FT DOMAIN 15..244 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 29 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000250|UniProtKB:P0A9N4" FT BINDING 33 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000250|UniProtKB:P0A9N4" FT BINDING 35..37 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P0A9N4" FT BINDING 36 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000250|UniProtKB:P0A9N4" FT BINDING 79 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P0A9N4" FT BINDING 134..136 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P0A9N4" FT BINDING 207 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P0A9N4" SQ SEQUENCE 251 AA; 28499 MW; 892A603E273F6C89 CRC64; MLKGHLHSVE SLGTVDGPGL RYILFTQGCL LRCLYCHNPD TWKISEPSRE VTVDEMVNEI LPYKPYFDAS GGGVTVSGGE PLLQMPFLEK LFAELKENGV HTCLDTSAGC ANDTKAFQRH FEELQKHTDL ILLDIKHIDN DKHIRLTGKP NTHILNFARK LSDMKQPVWI RHVLVPGYSD DKDDLIKLGE FINSLDNVEK FEILPYHQLG VHKWKTLGIA YELEDVEAPD DEAVKAAYRY VNFKGKIPVE L //