ID A8FTZ6_SHESH Unreviewed; 760 AA.
AC A8FTZ6;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
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=Ssed_1708 {ECO:0000313|EMBL:ABV36319.1};
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV36319.1, ECO:0000313|Proteomes:UP000002015};
RN [1] {ECO:0000313|EMBL:ABV36319.1, ECO:0000313|Proteomes:UP000002015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV36319.1,
RC ECO:0000313|Proteomes:UP000002015};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-2007) 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}.
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DR EMBL; CP000821; ABV36319.1; -; Genomic_DNA.
DR RefSeq; WP_012142055.1; NC_009831.1.
DR AlphaFoldDB; A8FTZ6; -.
DR STRING; 425104.Ssed_1708; -.
DR KEGG; sse:Ssed_1708; -.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_023898_0_0_6; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000002015; Chromosome.
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:UP000002015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 6..625
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 632..760
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 419
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 420
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; 84507 MW; C9F8C515A9DD1A3E CRC64;
MTEKTEQFAN AWAGFASGDW KTEVNVRDFI QANYTPYEGD EAFLAEATPA TTQLWDKVMV
GIKQENSTHA PVDFDTKKVS TITSHEAGYI EQELETIVGL QTEAPLKRAM LPNGGIRMVE
GSCKAYGREL DSDVKYVYSE LRKTHNQGVF DIYTPEIMRC RKSGVLTGLP DAYGRGRIIG
DYRRIALYGI DYLMADKFAQ FGSLQAGFEA GEDLSSTMQL REEIAEQHRA LGQMKQMAAS
YGFDISKPAT NAQEAIQWTY FGYLAAVKSQ NGAAMSLGRT SSFLDVFIER DLKNGTLTEE
QAQEMVDHFV MKLRMVRFLR TPEYDELFSG DPIWATESIA GMGVDGRTLV TKSSFRFLHT
LYNMGASPEP NITVLWSEKL PLPFKKYCAK VSIDTSSIQY ENDDLMRPDF ASDDYAIACC
VSPMIVGQHM QFFGARANLA KTMLYAINGG LDEKLKTQIG PKFDAITSEV LDFDDVMGRL
DTMMDWLATQ YVTALNSIHY MHDKYSYEAA LMALHDRDVR RTMACGIAGL SIAADSLSAI
KFAKVKPIRD EHGIAVDFDI EGDYPKFGNN DARVDDLATE LVERFMAKIR SMKMYRNAIP
TQSILTITSN VVYGKKTGTT PDGRPAGAPF APGANPMHGR DEKGAVASLT SVAKLPFAHA
QDGISYTFSI VPNALGKDED GRRANLAALM DGYFAHNDSR EGGQHLNVNV MNREMLEDAV
VNPDKYPQLT IRVSGYAVRF NALTPEQQQD VITRTFTQGM
//
