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
//