ID A0A0M1JSS3_9CYAN Unreviewed; 760 AA.
AC A0A0M1JSS3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ORFNames=AM228_13720 {ECO:0000313|EMBL:KOR36276.1};
OS Planktothricoides sp. SR001.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothricoides.
OX NCBI_TaxID=1705388 {ECO:0000313|EMBL:KOR36276.1, ECO:0000313|Proteomes:UP000037054};
RN [1] {ECO:0000313|Proteomes:UP000037054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR001 {ECO:0000313|Proteomes:UP000037054};
RA Tan B., Te S.H., Thompson J., Gin K.;
RT "Draft Genome of Planktothricoides sp. SR001.";
RL Submitted (AUG-2015) 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 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}.
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:KOR36276.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LIUQ01000020; KOR36276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M1JSS3; -.
DR STRING; 1705388.AM228_13720; -.
DR PATRIC; fig|1705388.3.peg.3118; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000037054; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037054};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 14..630
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 637..760
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 424
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 425
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 735
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 760 AA; 85728 MW; 64D0411E71982AEE CRC64;
MIMHRERPTQ LTLQNLGQIC QQWEGFTGGK WTREVNIQNF IQQNYTPYLG DESFLKTATE
RTKSLWQEVL ELMKVEREKG VLDVDTKVPS SITAHAPGYI NQNQEIIVGL QTEKPLKRAI
MPLGGIRVVK ASLEAYNYQL DPETEEIFTK YRKTHNDGVF DAYTSEMRLA RHAGIITGLP
DAYGRGRIIG DYRRVALYGI DRLTLDKKHQ LSALEVDVID ESVIRLREEV NEQIKALVEL
KEMAAAYGFD ISVPAANAKE AVQWTYFAYL GAVKEQNGAA MSLGRVSNFL DIYFERDFQK
GILTEAEAQE IIDDFVIKLR MVRFLRSPEY NQLFSGDPVW VTEAIGGIGE DGRPLVTKSS
YRFLHTLDNL GAAPEPNLTV LWSEFLPKKF KNFCAKMSVT TSSIQYENDD LMRPQFGDDY
GIACCVSAME IGKKMQFFGA RVNLAKALLY AINGGKDEKS GQQIGLKVDP ITADYLDYDE
VVAKFDVMMA WLAKTYVNTL NTIHYMHDKY CYERLEMALH DLNVQRTMAC GIAGLSVVAD
ALSAIKYAKV KVIRNDSGLA VDYQIEGDYP KFGNNDYRVD EIAVNLVRQV MNNLRKHKTY
RDAIPTQSVL TITSNVVYGK ATGNTPDGRK AGEPFAPGAN PMHGRDTKGA IASMSSVAKL
PYDDAQDGIS YTFTIVPEAL GKTEESRINN LVGLLDGYFH ETGHHINVNV LNRETLHDAM
EHPEKYPQLT IRVSGYAVNF IKLTREQQMD VITRTFHDRF
//
