ID   PFL_CHLRE               Reviewed;         195 AA.
AC   P37836;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Formate acetyltransferase;
DE            EC=2.3.1.54;
DE   AltName: Full=Pyruvate formate-lyase;
DE   Flags: Fragment;
GN   Name=PFL;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=137c / CC-125;
RA   Dumont F., Joris B., Gumusboga A., Bruyninx M., Loppes R.;
RT   "Isolation and characterization of cDNA sequences controlled by inorganic
RT   phosphate in Chlamydomonas reinhardtii.";
RL   Plant Sci. 89:55-67(1993).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X66410; CAA47041.1; -; mRNA.
DR   PIR; S24997; S24997.
DR   AlphaFoldDB; P37836; -.
DR   SMR; P37836; -.
DR   STRING; 3055.EDP09457; -.
DR   PRIDE; P37836; -.
DR   ProMEX; P37836; -.
DR   EnsemblPlants; PNW88792; PNW88792; CHLRE_01g044800v5.
DR   Gramene; PNW88792; PNW88792; CHLRE_01g044800v5.
DR   eggNOG; ENOG502QSG9; Eukaryota.
DR   BRENDA; 2.3.1.54; 1318.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008861; F:formate C-acetyltransferase activity; IEA:UniProtKB-EC.
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   PROSITE; PS00850; GLY_RADICAL_1; 1.
DR   PROSITE; PS51149; GLY_RADICAL_2; 1.
DR   PROSITE; PS51554; PFL; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Cytoplasm; Organic radical; Transferase.
FT   CHAIN           <1..195
FT                   /note="Formate acetyltransferase"
FT                   /id="PRO_0000166696"
FT   DOMAIN          1..64
FT                   /note="PFL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT   DOMAIN          71..195
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT   REGION          54..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         170
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT   NON_TER         1
SQ   SEQUENCE   195 AA;  21350 MW;  55F4DCE415735D6A CRC64;
     GSFPKYGNDD DRVDEIAEWV VSTFSSKLAK QHTYRNSVPT LSVLTITSNV VYGKKTGSTP
     DGRKKGEPFA PGANPLHGRD AHGALASLNS VAKLPYTMCL DGISNTFSLI PQVLGRGGEH
     ERATNLASIL DGYFANGGHH INVNVLNRSM LMDAVEHPEK YPNLTIRVSG YAVHFARLTR
     EQQLEVIART FHDTM