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-MAY-2013, entry version 56.
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 (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; 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 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; ILESYGH; -.
DR ProtClustDB; CLSK884495; -.
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: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) (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
//
