ID A0A1Q5PJC4_9ACTO Unreviewed; 701 AA.
AC A0A1Q5PJC4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=formate C-acetyltransferase {ECO:0000256|ARBA:ARBA00013214};
DE EC=2.3.1.54 {ECO:0000256|ARBA:ARBA00013214};
GN ORFNames=BSR29_08405 {ECO:0000313|EMBL:OKL45991.1};
OS Boudabousia liubingyangii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Boudabousia.
OX NCBI_TaxID=1921764 {ECO:0000313|EMBL:OKL45991.1, ECO:0000313|Proteomes:UP000186785};
RN [1] {ECO:0000313|EMBL:OKL45991.1, ECO:0000313|Proteomes:UP000186785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VUL4_2 {ECO:0000313|EMBL:OKL45991.1,
RC ECO:0000313|Proteomes:UP000186785};
RA Meng X.;
RT "Actinomyces gypaetusis sp. nov. isolated from the vulture Gypaetus
RT barbatus in Qinghai Tibet Plateau China.";
RL Submitted (NOV-2016) 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:OKL45991.1}.
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DR EMBL; MQSV01000007; OKL45991.1; -; Genomic_DNA.
DR RefSeq; WP_073709858.1; NZ_MQSU01000002.1.
DR AlphaFoldDB; A0A1Q5PJC4; -.
DR STRING; 1921764.BSR28_04420; -.
DR OrthoDB; 9803969at2; -.
DR Proteomes; UP000186785; 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:UP000186785};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OKL45991.1}.
FT DOMAIN 10..628
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 635..701
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
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 701 AA; 77895 MW; 16B65937366003DB CRC64;
MAKDDTAQVE ESAALPEAWE GFVPGNWCEN IDVRDFIQLN YTPYEGDASF LSGPTEKTLR
TWETLEKEYL SVERAKRVYD VDTKTPADVD AFGAGYISED DDVIVGLQTD VPLKRAMMPN
GGWRMVETAI REAGKEPDPE IKKIFTQYRK THNDAVFDIY TPRIRAARSS HIITGLPDAY
GRGRIIGDYR RVALYGVDKL IEEKQKDKDL VADKPFSEHW CRYREEHAEQ IKALKKLKNM
AASYGFDISG PATNAKEAVQ WTYFGYLASV KSQDGAAMSI GRLSGFFDSY FERDFKRGIL
TEDEAQEIID ALVIKLRIVR FLRTIDYDAI FSGDPYWATW SDGGMGQDGR TLVTKTSFRL
LQTLRNLGPA PEPNITLFWN KALPQGYKDF CALISIETSS VQYEADEQIR EHWGDDAAIA
CCVSPMQVGK QMQFFGARVN AAKALLYAIN GGRDEMSGKQ VVNGYEPVQG DGPLDFEEVW
AKYEDMLDWV VGTYVEALNI IHFCHDRYAY ESIEMALHDS EIVRTMGCGI AGLSIVADSL
SAIRYAKVTP IRDETGLVVD YKTEGDFPVY GNDDDRADDI AATVVHTIMS KIKAIPMYRD
AIPTQSVLTI TSNVVYGKAT GSFPSGHKAG TPFAPGANPE NGMDTHGMLA SMMSVGKLDY
DDALDGISLT NTITPSGLGR TLDEQIKNLV GIMDAGFIPQ A
//