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Database: UniProt
Entry: Q99WZ6
LinkDB: Q99WZ6
Original site: Q99WZ6 
ID   PFLA_STAAM              Reviewed;         251 AA.
AC   Q99WZ6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   09-JUL-2014, entry version 80.
DE   RecName: Full=Pyruvate formate-lyase-activating enzyme;
DE            Short=PFL-activating enzyme;
DE            EC=1.97.1.4;
GN   Name=pflA; OrderedLocusNames=SAV0227;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA   Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA   Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA   Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA   Ogasawara N., Hayashi H., Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus
RT   aureus.";
RL   Lancet 357:1225-1240(2001).
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
CC       produce 5'-deoxy-adenosine (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + dihydroflavodoxin +
CC       [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-
CC       methionine + flavodoxin semiquinone + [formate C-
CC       acetyltransferase]-glycin-2-yl radical.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with
CC       3 cysteines and an exchangeable S-adenosyl-L-methionine (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes
CC       family.
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DR   EMBL; BA000017; BAB56389.1; -; Genomic_DNA.
DR   RefSeq; NP_370751.1; NC_002758.2.
DR   ProteinModelPortal; Q99WZ6; -.
DR   SMR; Q99WZ6; 71-207.
DR   STRING; 158878.SAV0227; -.
DR   PRIDE; Q99WZ6; -.
DR   EnsemblBacteria; BAB56389; BAB56389; SAV0227.
DR   GeneID; 1120185; -.
DR   KEGG; sav:SAV0227; -.
DR   PATRIC; 19561064; VBIStaAur52173_0229.
DR   eggNOG; COG1180; -.
DR   HOGENOM; HOG000011458; -.
DR   KO; K04069; -.
DR   OMA; WEMETNK; -.
DR   OrthoDB; EOG64FKHC; -.
DR   PhylomeDB; Q99WZ6; -.
DR   BioCyc; SAUR158878:GJJ5-228-MONOMER; -.
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   InterPro; IPR012838; PFL_activating.
DR   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   TIGRFAMs; TIGR02493; PFLA; 1.
DR   PROSITE; PS01087; RADICAL_ACTIVATING; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Carbohydrate metabolism; Complete proteome; Cytoplasm;
KW   Glucose metabolism; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW   S-adenosyl-L-methionine.
FT   CHAIN         1    251       Pyruvate formate-lyase-activating enzyme.
FT                                /FTId=PRO_0000271712.
FT   METAL        29     29       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        33     33       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        36     36       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
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
//
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