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Database: UniProt
Entry: U2RRK0_9ACTN
LinkDB: U2RRK0_9ACTN
Original site: U2RRK0_9ACTN 
ID   U2RRK0_9ACTN            Unreviewed;       701 AA.
AC   U2RRK0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=formate C-acetyltransferase {ECO:0000256|ARBA:ARBA00013214};
DE            EC=2.3.1.54 {ECO:0000256|ARBA:ARBA00013214};
GN   ORFNames=HMPREF0682_2625 {ECO:0000313|EMBL:ERK53332.1};
OS   Propionibacterium acidifaciens F0233.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=553198 {ECO:0000313|EMBL:ERK53332.1, ECO:0000313|Proteomes:UP000017052};
RN   [1] {ECO:0000313|EMBL:ERK53332.1, ECO:0000313|Proteomes:UP000017052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0233 {ECO:0000313|EMBL:ERK53332.1,
RC   ECO:0000313|Proteomes:UP000017052};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:ERK53332.1}.
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DR   EMBL; ACVN02000239; ERK53332.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2RRK0; -.
DR   Proteomes; UP000017052; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ERK53332.1}.
FT   DOMAIN          9..624
FT                   /note="PFL"
FT                   /evidence="ECO:0000259|PROSITE:PS51554"
FT   DOMAIN          631..701
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000259|PROSITE:PS51149"
FT   ACT_SITE        417
FT                   /note="S-acetylcysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT   ACT_SITE        418
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
SQ   SEQUENCE   701 AA;  78271 MW;  1CA62DF5EDEA2FF2 CRC64;
     MTITEADAVQ TENPWHDFVE GPWTEAIDVR DFIQRNYTPY EGDASFLAGP TEKTLRVWDH
     LEKNYLSEER KRRVYDVDTH TPNDIDAFGP GYICDDDDVI VGLQTDVPLK RAMMPNGGWR
     MVETAIKEAG KEVDPEVKKI FTKYRKTHND AVFDIYTPRI RAARSSHIIT GLPDAYGRGR
     IIGDYRRVAL YGVDKLIEWK QADKDKVTDE PFSEHWARYR EEHAEQIKAL KKLKTMAAGY
     GFDLSAPARS AKEAVQWTYF GYLASVKSQD GAAMSIGRLS AFLDCYFERD LRAGLITESE
     AQEMIDAIVL KLRIVRFLRT IDYDQIFSGD PYWATWSDAG FGDDGRAMVT KTSFRLLQTL
     RNLGPAPEPN ITIFWDKRLP KGYKDFCAAI SIETSAIQYE SDRDIRAHWG DDAAIACCVS
     PMRVGKQMQF FGARVNSAKA LLYAINGGRD EMSGKLVADG FESVSGDGPL DFDDVWERYE
     KMLDWVVGTY VEALNIIHYC HDRYAYEAIE MALHDSDIVR TLGCGIAGLS IVADSLSAIK
     YATVTPVRDE TGLVVDYITE GDFPKYGNDD DRADEIASTV VHTIMSKIRE IKLYRDAIPT
     QSVLTITSNV VYGKATGAFP SGHEKGTPFA PGANPENGMD THGMVASMLS VGKLDYNDAL
     DGISLTNTIT PTGLGRDKDE QVANLVGILD AGFLPNDCTC Y
//
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