ID S1NI76_9ENTE Unreviewed; 742 AA.
AC S1NI76;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Formate acetyltransferase {ECO:0000256|ARBA:ARBA00013897, ECO:0000256|RuleBase:RU368075};
DE EC=2.3.1.54 {ECO:0000256|ARBA:ARBA00013214, ECO:0000256|RuleBase:RU368075};
DE AltName: Full=Pyruvate formate-lyase {ECO:0000256|ARBA:ARBA00031063, ECO:0000256|RuleBase:RU368075};
GN ORFNames=OMK_00497 {ECO:0000313|EMBL:EOT43144.1};
OS Enterococcus dispar ATCC 51266.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1139219 {ECO:0000313|EMBL:EOT43144.1, ECO:0000313|Proteomes:UP000014127};
RN [1] {ECO:0000313|EMBL:EOT43144.1, ECO:0000313|Proteomes:UP000014127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51266 {ECO:0000313|EMBL:EOT43144.1,
RC ECO:0000313|Proteomes:UP000014127};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus dispar ATCC_51266 (Illumina only
RT assembly).";
RL Submitted (MAR-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 ECO:0000256|RuleBase:RU368075};
CC -!- PATHWAY: Fermentation; pyruvate fermentation; formate from pyruvate:
CC step 1/1. {ECO:0000256|ARBA:ARBA00004809,
CC 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:EOT43144.1}.
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DR EMBL; AHYR01000003; EOT43144.1; -; Genomic_DNA.
DR RefSeq; WP_016171703.1; NZ_KE136354.1.
DR AlphaFoldDB; S1NI76; -.
DR PATRIC; fig|1139219.3.peg.467; -.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_023898_0_0_9; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000014127; 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|ARBA:ARBA00022526,
KW ECO:0000256|RuleBase:RU368075};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW ECO:0000256|PIRSR:PIRSR000379-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000014127};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 1..612
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 619..742
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 406
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 407
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 717
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 742 AA; 83601 MW; A7C1B3049A635C9A CRC64;
MEQWNGFKGK AWQNEVNVRD FIQANYTQFD GTDEFLAGPT EATTKLWDQV MELNQQERDN
GGVLDMDTKV VSTITSHGPG YLNKELETVV GFQTEKPFKR SLQPFGGIRM SEQAAEAYGY
EIDPEISHIF RDYRKTHNQG VFDAYTPEMR AARRSGVITG LPDAYGRGRI IGDYRRVALY
GVDFLIKEKQ KDLFNCGNGT MSDDVIRQRE ELNEQLRALN ELKELGTIYG FDISQPATNA
KEAFQWLYLG YLAAIKEQNG AAMSLGRTST FLDIYVERDL QNGVLTEEEA QEIVDHFVMK
LRLVKFARTP DYNALFSGDP TWVTESIGGI GEDGRHMVTK NSFRFLHTLS NLGPAPEPNL
TVLWSTRLPH NFKTFCAKMS IQTSAIQYEN DDVMRPHWGD DYGIACCVSA MRIGKQMQFF
GARANLAKTL LYAINGGVDE KSKAQVGPKY QPITSEYLAY DEVVEKYDAM MDWITELYLN
TLNIIHYMHD KYSYERIEMA LQDTDILRTM ATGIAGFSVA VDSLSAIKYA KVKTVRDENG
IVEDYIIEGD YPKYGNNDDR VDEIAVNLLK TFMTKVKRNK TYRDAKHTTS ILTITSNVVY
GKKTGNTPDG RRAGQPFAPG ANPMHGRDTH GALASLSSVA KIPYDYSLDG ISNTFSIVPK
ALGRDEATQE ENLATMLDGY AAKGGHHLNI NVFNRDTLLD AQAHPEKYPQ LTIRVSGYAV
NFIKLTKEQQ DDVIARTMHE SM
//
