ID E3HCG6_ILYPC Unreviewed; 744 AA.
AC E3HCG6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Formate acetyltransferase {ECO:0000256|RuleBase:RU368075};
DE EC=2.3.1.54 {ECO:0000256|RuleBase:RU368075};
DE AltName: Full=Pyruvate formate-lyase {ECO:0000256|RuleBase:RU368075};
GN OrderedLocusNames=Ilyop_2179 {ECO:0000313|EMBL:ADO83942.1};
OS Ilyobacter polytropus (strain ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1).
OG Plasmid pILYOP01 {ECO:0000313|EMBL:ADO83942.1,
OG ECO:0000313|Proteomes:UP000006875}.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Ilyobacter.
OX NCBI_TaxID=572544 {ECO:0000313|EMBL:ADO83942.1, ECO:0000313|Proteomes:UP000006875};
RN [1] {ECO:0000313|EMBL:ADO83942.1, ECO:0000313|Proteomes:UP000006875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1
RC {ECO:0000313|Proteomes:UP000006875};
RC PLASMID=pILYOP01 {ECO:0000313|Proteomes:UP000006875};
RX PubMed=21304735; DOI=10.4056/sigs.1273360;
RA Sikorski J., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Yasawong M.,
RA Rohde M., Pukall R., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ilyobacter polytropus type strain (CuHbu1).";
RL Stand. Genomic Sci. 3:304-314(2010).
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 ECO:0000256|RuleBase:RU368075};
CC -!- PATHWAY: Fermentation; pyruvate fermentation; formate from pyruvate:
CC step 1/1. {ECO:0000256|RuleBase:RU368075}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU368075}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU368075}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC subfamily. {ECO:0000256|ARBA:ARBA00008375,
CC ECO:0000256|RuleBase:RU368075}.
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DR EMBL; CP002282; ADO83942.1; -; Genomic_DNA.
DR AlphaFoldDB; E3HCG6; -.
DR KEGG; ipo:Ilyop_2179; -.
DR HOGENOM; CLU_023898_0_0_0; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000006875; Plasmid pILYOP01.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008861; F:formate C-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01678; PFL1; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005949; Form_AcTrfase.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR004184; PFL_dom.
DR NCBIfam; TIGR01255; pyr_form_ly_1; 1.
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; PS00850; GLY_RADICAL_1; 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 ECO:0000256|RuleBase:RU368075};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU368075};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368075};
KW Glucose metabolism {ECO:0000256|RuleBase:RU368075};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW ECO:0000256|PIRSR:PIRSR000379-2}; Plasmid {ECO:0000313|EMBL:ADO83942.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006875};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 1..614
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 621..744
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT REGION 605..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 408
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 409
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 719
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 744 AA; 85104 MW; BE49FB263F0BB264 CRC64;
MKKFDPWSDF KEGKWHKNID VRDFIQKNYT PYEGDESFLS GPTERTRELF EKFEELRKIE
LERKGVVDIN TDTVSSLLTY DAGYLDKDKE IIVGIQTDKP LKRGVNPFGG IKMTRQAVEA
YGYELDQKIE DYFAYKTTHN DGVFRVYNEA MKTARSTGMI TGLPDAYGRG RIIGDYRRVS
LYGVDRLLDE KKKDKIIYGR KKMTEENIRL LEELYKQIDF LKKMKDMAKL YGYDISAPAK
DSKEAVQWLY FAYLASVKEQ NGAAMSLGRV STFLDIYFQR DIKRGILTEK DSQEIIDDFV
LKLRMVRQLR TPEYNELFAG DPNWITEVIG GTGTDGRTMV TKSSYRFLNS LYTLAPAPEP
NLTVLWSETL PENFKRFCAK VSMDTDSIQY ENDDLMRSRY GDDYGIACCV SAMKIGKQMQ
YFGARCNMPK ILLMALNGGK DEVSGKQTGP EMESFQSKPL NYEDVMKRLK LYREWLCELY
VNTMNIIHFM HDKYSYEKTQ MALHDTEVER SMAFGMAGLS VVADSLSAIK YAKVTPVKNE
EGIITDFDVE GDFPKFGNND DRVDSIAAEL TEDFIKDLKK HETYRNAEHT LSILTITSNV
VYGKKTGSTP DGRKKGEPFA PGANPMHNRE KKGALASLTS VAKIPYDACR DGISCTFSIP
PKTLGKTEED RKTILTSILD GYFSQNAHHL NVNVLDKEKL EDAMIHPEKY PNLTIRVSGY
AVNFNSLSIE QQKEVISRTF HNEI
//
