ID PFL_STRMU Reviewed; 775 AA.
AC Q59934;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Formate acetyltransferase;
DE EC=2.3.1.54;
DE AltName: Full=Pyruvate formate-lyase;
GN Name=pfl; OrderedLocusNames=SMU_402;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GS-5;
RX PubMed=8550181; DOI=10.1128/iai.64.2.385-391.1996;
RA Yamamoto Y., Sato Y., Takahashi-Abbe S., Abbe K., Yamada T., Kizaki H.;
RT "Cloning and sequence analysis of the pfl gene encoding pyruvate formate-
RT lyase from Streptococcus mutans.";
RL Infect. Immun. 64:385-391(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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 -!- PATHWAY: Fermentation; pyruvate fermentation; formate from pyruvate:
CC step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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}.
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DR EMBL; D50491; BAA09085.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58156.1; -; Genomic_DNA.
DR RefSeq; NP_720850.1; NC_004350.2.
DR RefSeq; WP_002262619.1; NC_004350.2.
DR AlphaFoldDB; Q59934; -.
DR SMR; Q59934; -.
DR STRING; 210007.SMU_402; -.
DR KEGG; smu:SMU_402; -.
DR PATRIC; fig|210007.7.peg.352; -.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_023898_0_0_9; -.
DR OrthoDB; 9803969at2; -.
DR PhylomeDB; Q59934; -.
DR BioCyc; MetaCyc:MONOMER-13094; -.
DR SABIO-RK; Q59934; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000002512; 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 Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005949; Form_AcTrfase.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR004184; PFL_dom.
DR NCBIfam; TIGR01255; pyr_form_ly_1; 1.
DR PANTHER; PTHR30191; FORMATE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR30191:SF8; FORMATE ACETYLTRANSFERASE; 1.
DR Pfam; PF01228; Gly_radical; 1.
DR Pfam; PF02901; PFL-like; 1.
DR PIRSF; PIRSF000379; For_Ac_trans_1; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS00850; GLY_RADICAL_1; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
DR PROSITE; PS51554; PFL; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Carbohydrate metabolism; Cytoplasm; Glucose metabolism;
KW Organic radical; Reference proteome; Transferase.
FT CHAIN 1..775
FT /note="Formate acetyltransferase"
FT /id="PRO_0000166695"
FT DOMAIN 9..626
FT /note="PFL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT DOMAIN 642..762
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 737
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT CONFLICT 43
FT /note="D -> G (in Ref. 1; BAA09085)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="P -> S (in Ref. 1; BAA09085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 87606 MW; 6ED30F2365F43D7C CRC64;
MATVKTNTDV FEKAWEGFKG TDWKDRASIS RFVQDNYTPY DGDESFLAGP TERSLHIKKV
VEETKAHYEE TRFPMDTRIT SIADIPAGYI DKENELIFGI QNDELFKLNF MPKGGIRMAE
TALKEHGYEP DPAVHEIFTK YATTVNDGIF RAYTSNIRRA RHAHTVTGLP DAYSRGRIIG
VYARLALYGA DYLMQEKVND WNSIAEIDEE SIRLREEINL QYQALGEVVR LGDLYGLDVR
KPAMNVKEAI QWINIAFMAV CRVINGAATS LGRVPIVLDI FAERDLARGT FTESEIQEFV
DDFVMKLRTV KFARTKAYDE LYSGDPTFIT TSMAGMGADG RHRVTKMDYR FLNTLDNIGN
APEPNLTVLW SSKLPYPFRH YCMSMSHKHS SIQYEGVTTM AKEGYGEMSC ISCCVSPLDP
ENEDRRHNLQ YFGARVNVLK ALLTGLNGGY DDVHKDYKVF DVEPIRDEVL DFETVKANFE
KALDWLTDTY VDAMNIIHYM TDKYNYEAVQ MAFLPTRVKA NMGFGICGFS NTVDSLSAIK
YATVKPIRDE DGYIYDYETV GNFPRYGEDD DRVDSIAEWL LEAFHTRLAR HKLYKDSEAT
VSLLTITSNV AYSKQTGNSP VHKGVYLNED GSVNLSKVEF FSPGANPSNK ASGGWLQNLN
SLKKLDFAHA NDGISLTTQV SPKALGKTFD EQVANLVTIL DGYFEGGGQH VNLNVMDLKD
VYDKIMNGED VIVRISGYCV NTKYLTKEQK TELTQRVFHE VLSMDDAATD LVNNK
//
