PFLB_STAAC
ID PFLB_STAAC Reviewed; 749 AA.
AC Q5HJF4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Formate acetyltransferase;
DE EC=2.3.1.54;
DE AltName: Full=Pyruvate formate-lyase;
GN Name=pflB; OrderedLocusNames=SACOL0204;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14617657; DOI=10.1128/jb.185.23.6928-6937.2003;
RA Kohler C., von Eiff C., Peters G., Proctor R.A., Hecker M., Engelmann S.;
RT "Physiological characterization of a heme-deficient mutant of
RT Staphylococcus aureus by a proteomic approach.";
RL J. Bacteriol. 185:6928-6937(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + formate = CoA + pyruvate; Xref=Rhea:RHEA:11844,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15740, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.1.54;
CC -!- ACTIVITY REGULATION: Activated by pfl-activating enzyme under anaerobic
CC conditions via generation of an organic free radical (Probable).
CC Exposure of activated pfl to oxygen results in a cleavage at the
CC glycine residue harboring its organic radical with loss of the 25 C-
CC terminal amino acids. {ECO:0000305}.
CC -!- PATHWAY: Fermentation; pyruvate fermentation; formate from pyruvate:
CC step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14617657}.
CC -!- MISCELLANEOUS: Several mechanisms have been proposed based on complexes
CC formed with substrate analogs. After activation by the glycine radical,
CC the cysteine radical, Cys-414, can abstract hydrogen atoms from the
CC other active site cysteine, Cys-413, and from coenzyme A, and it can
CC also transfer hydrogen atoms to product radicals. The other active site
CC cysteine can attack the central carbonyl of pyruvate and covalently
CC bind the product acetyl group (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC subfamily. {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; CP000046; AAW37500.1; -; Genomic_DNA.
DR RefSeq; WP_000894660.1; NC_002951.2.
DR AlphaFoldDB; Q5HJF4; -.
DR SMR; Q5HJF4; -.
DR PRIDE; Q5HJF4; -.
DR EnsemblBacteria; AAW37500; AAW37500; SACOL0204.
DR KEGG; sac:SACOL0204; -.
DR HOGENOM; CLU_023898_0_0_9; -.
DR OMA; PYGGIKM; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000000530; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008861; F:formate C-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01678; PFL1; 1.
DR InterPro; IPR005949; Form_AcTrfase.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR004184; PFL_dom.
DR Pfam; PF01228; Gly_radical; 1.
DR Pfam; PF02901; PFL-like; 1.
DR TIGRFAMs; TIGR01255; pyr_form_ly_1; 1.
DR PROSITE; PS00850; GLY_RADICAL_1; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
DR PROSITE; PS51554; PFL; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Carbohydrate metabolism; Cytoplasm; Glucose metabolism;
KW Organic radical; Transferase.
FT CHAIN 1..749
FT /note="Formate acetyltransferase"
FT /id="PRO_0000271722"
FT DOMAIN 3..619
FT /note="PFL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT DOMAIN 626..749
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT ACT_SITE 413
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 414
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 724
FT /note="Glycine radical"
FT /evidence="ECO:0000305"
SQ SEQUENCE 749 AA; 84862 MW; F38EEC2D41FF03A5 CRC64;
MLETNKNHAT AWQGFKNGRW NRHVDVREFI QLNYTLYEGN DSFLAGPTEA TSKLWEQVMQ
LSKEERERGG MWDMDTKVAS TITSHDAGYL DKDLETIVGV QTEKPFKRSM QPFGGIRMAK
AACEAYGYEL DEETEKIFTD YRKTHNQGVF DAYSREMLNC RKAGVITGLP DAYGRGRIIG
DYRRVALYGV DFLMEEKMHD FNTMSTEMSE DVIRLREELS EQYRALKELK ELGQKYGFDL
SRPAENFKEA VQWLYLAYLA AIKEQNGAAM SLGRTSTFLD IYAERDLKAG VITESEVQEI
IDHFIMKLRI VKFARTPDYN ELFSGDPTWV TESIGGVGID GRPLVTKNSF RFLHSLDNLG
PAPEPNLTVL WSVRLPDNFK TYCAKMSIKT SSIQYENDDI MRESYGDDYG IACCVSAMTI
GKQMQFFGAR ANLAKTLLYA INGGKDEKSG AQVGPNFEGI NSEVLEYDEV FKKFDQMMDW
LAGVYINSLN VIHYMHDKYS YERIEMALHD TEIVRTMATG IAGLSVAADS LSAIKYAQVK
PIRNEEGLVV DFEIEGDFPK YGNNDDRVDD IAVDLVERFM TKLRSHKTYR DSEHTMSVLT
ITSNVVYGKK TGNTPDGRKA GEPFAPGANP MHGRDQKGAL SSLSSVAKIP YDCCKDGISN
TFSIVPKSLG KEPEDQNRNL TSMLDGYAMQ CGHHLNINVF NRETLIDAME HPEEYPQLTI
RVSGYAVNFI KLTREQQLDV ISRTFHESM
