ID   A0A022KWG6_9MICO        Unreviewed;       709 AA.
AC   A0A022KWG6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=formate C-acetyltransferase {ECO:0000256|ARBA:ARBA00013214};
DE            EC=2.3.1.54 {ECO:0000256|ARBA:ARBA00013214};
GN   ORFNames=D641_0104970 {ECO:0000313|EMBL:EYT50134.1};
OS   Brachybacterium muris UCD-AY4.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=1249481 {ECO:0000313|EMBL:EYT50134.1, ECO:0000313|Proteomes:UP000019754};
RN   [1] {ECO:0000313|EMBL:EYT50134.1, ECO:0000313|Proteomes:UP000019754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-AY4 {ECO:0000313|EMBL:EYT50134.1,
RC   ECO:0000313|Proteomes:UP000019754};
RX   PubMed=23516213;
RA   Lo J.R., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT   "Draft genome sequence of an Actinobacterium, Brachybacterium muris strain
RT   UCD-AY4.";
RL   Genome Announc. 1:E0008613-E0008613(2013).
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         Evidence={ECO:0000256|ARBA:ARBA00001179};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC       subfamily. {ECO:0000256|ARBA:ARBA00008375}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00493}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYT50134.1}.
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DR   EMBL; AORC01000005; EYT50134.1; -; Genomic_DNA.
DR   RefSeq; WP_031306949.1; NZ_AORC01000005.1.
DR   AlphaFoldDB; A0A022KWG6; -.
DR   STRING; 1249481.D641_0104970; -.
DR   HOGENOM; CLU_023898_0_0_11; -.
DR   OrthoDB; 9803969at2; -.
DR   Proteomes; UP000019754; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR001150; Gly_radical.
DR   InterPro; IPR004184; PFL_dom.
DR   PANTHER; PTHR30191; FORMATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR30191:SF0; FORMATE ACETYLTRANSFERASE 1; 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; PS51149; GLY_RADICAL_2; 1.
DR   PROSITE; PS51554; PFL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Organic radical {ECO:0000256|ARBA:ARBA00022818};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019754};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EYT50134.1}.
FT   DOMAIN          10..630
FT                   /note="PFL"
FT                   /evidence="ECO:0000259|PROSITE:PS51554"
FT   DOMAIN          637..709
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000259|PROSITE:PS51149"
FT   REGION          628..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        421
FT                   /note="S-acetylcysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT   ACT_SITE        422
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
SQ   SEQUENCE   709 AA;  78727 MW;  43472E098BFC8723 CRC64;
     MTSATTERPT DALAGGDAWE GFAPGPWQES IDLRDFILRN YTPYDGDASF LAGPTEKTLK
     VWDHLEKNYL SEERRRRVYD VDTKTPADID AFPAGYICPE DDVIVGLQTD VPLKRAMMPN
     GGWRMVETAI KEAGKEPDPE IKKVFTKYRK THNEGVFDIY TPRIRAARSS HIITGLPDAY
     GRGRIIGDYR RLALYGADFL IAEKMAAKDA VADQPFSEHW ARYREEHSEQ IKALKKLVTL
     GEIYGLDLKR PAATAQEAVQ WTYMAYLASV KSQDGAAMSL GRLSAFLDIY FERDLKAGKI
     TESDAQEIID ALVIKLRIVR FLRTIDYDQI FSGDPYWATW SDAGMTEDGR SQVTKTSFRL
     LQTLRNLGPA PEPNITVFWD PKLPEGYKEF CSAISIETSS IQYESDEQIR DRWGDDAAIA
     CCVSPMKVGK QMQFFGARVN AGKALLYAIN GGRDEISGKQ VTEEGEFTPV QGDGPLDFDD
     VWEKYEHMLD WVVGTYVEAL NIIHYSHDKY AYESIEMALH DSDIVRTMGC GIAGLSIVAD
     SLSAIKHATV TPVRDETGLI VDYITEGEFP RYGNDDDRAD DIAATIVHTV MQKIKEIPMY
     RDAIPTQSVL TITSNVVYGK ATGSFPSGHQ KGTPFSPGAN PENGADSHGM VASMLSVGKL
     DYNDALDGIS LTNTITPQGL GRTKDEQVKN LVGILDAGFV MDDDCTLTN
//