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Database: UniProt
Entry: Q2YV52
LinkDB: Q2YV52
Original site: Q2YV52 
ID   PFLA_STAAB              Reviewed;         251 AA.
AC   Q2YV52;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   01-OCT-2014, entry version 63.
DE   RecName: Full=Pyruvate formate-lyase-activating enzyme;
DE            Short=PFL-activating enzyme;
DE            EC=1.97.1.4;
GN   Name=pflA; OrderedLocusNames=SAB0165;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus
RT   aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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. {ECO:0000250}.
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes
CC       family. {ECO:0000305}.
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DR   EMBL; AJ938182; CAI79853.1; -; Genomic_DNA.
DR   RefSeq; YP_415675.1; NC_007622.1.
DR   ProteinModelPortal; Q2YV52; -.
DR   SMR; Q2YV52; 71-207.
DR   STRING; 273036.SAB0165; -.
DR   PRIDE; Q2YV52; -.
DR   EnsemblBacteria; CAI79853; CAI79853; SAB0165.
DR   GeneID; 3794307; -.
DR   KEGG; sab:SAB0165; -.
DR   PATRIC; 19521037; VBIStaAur92441_0187.
DR   eggNOG; COG1180; -.
DR   HOGENOM; HOG000011458; -.
DR   KO; K04069; -.
DR   OMA; VAMSNSE; -.
DR   OrthoDB; EOG64FKHC; -.
DR   BioCyc; SAUR273036:GJVS-167-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_0000271710.
FT   METAL        29     29       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000250}.
FT   METAL        33     33       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000250}.
FT   METAL        36     36       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000250}.
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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