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 01-MAY-2013, entry version 73.
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 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; ILESYGH; -.
DR ProtClustDB; CLSK884495; -.
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: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
//
