ID A0A154BQG9_ANASB Unreviewed; 741 AA.
AC A0A154BQG9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=AXX12_11105 {ECO:0000313|EMBL:KYZ75748.1};
OS Anaerosporomusa subterranea.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Anaerosporomusa.
OX NCBI_TaxID=1794912 {ECO:0000313|EMBL:KYZ75748.1, ECO:0000313|Proteomes:UP000076268};
RN [1] {ECO:0000313|EMBL:KYZ75748.1, ECO:0000313|Proteomes:UP000076268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU4 {ECO:0000313|EMBL:KYZ75748.1,
RC ECO:0000313|Proteomes:UP000076268};
RA Choi J.K., Shah M., Yee N.;
RT "Anaerosporomusa subterraneum gen. nov., sp. nov., a spore-forming obligate
RT anaerobe isolated from saprolite.";
RL Submitted (FEB-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 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:KYZ75748.1}.
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DR EMBL; LSGP01000020; KYZ75748.1; -; Genomic_DNA.
DR RefSeq; WP_066243472.1; NZ_LSGP01000020.1.
DR AlphaFoldDB; A0A154BQG9; -.
DR STRING; 1794912.AXX12_11105; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000076268; 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:UP000076268};
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..741
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 741 AA; 81571 MW; FD51D165722822D7 CRC64;
MDQWRGFTDG VWQTSVDVRD FIQKNYTPYE GDASFLAAAT FQTKRLWEEC TRLLKVERDS
DGVLDIDTEV VSTITSHAAG YIAKELELIV GLQTDAPLKR GVIVNGGVRM AEQACEAYGR
KLNPQISDIY HNHRKTHNTA VFEAYTEEMK QARRLGMITG LPDAYGRGRI IGDYRRIALY
GTERLIQEKQ DDLTALADSP MTEAVIRTRE EIAQQLHALA DLALMAKQYG FDISRPAEDA
QEAIQWLYFA YLGAIKEQNG AAMSLGRVST FLDIYIIRDL NEGRLDESGA QELIDQLIIK
LRLARHLRTP DYNELFAGDP LWVTEAIGGM GRDGRTLVTQ TSFRFLHTLA NLGPAPEPNL
TVLWSPALPE GFKQFSAAVS ISSSAIQYEN DELMRPEYGD DYAIACCVSA MTVGKQMQFF
GARANLAKAL LLAINGGRDE VSGEQIGPKL PLLTAETLDY DTVRVNLSIV LDWLTGLYVN
TMNLIHRMHD TYAYESLQMA LHDSEPGRLM AFGIAGLSVA ADSLSAIKHA KVKAVRDERG
IATGFEIAGD YPCYGNDDDR VDQIASGLCA EFSAKLKLHP AYRDAKHTLS ILTITSNVMY
GGKTGATPDG RQAGQPFAPG ANPMHGRDKR GALAAASSVA KLSYADCQDG ISYTFTVVPS
ALGKTKAARE KNLTALLDGY AIKGGHHINV NVLDRALLQA AMAKPEDYPQ LTIRVSGYAV
NFIKLSPLHQ QEVISRTFYE S
//
