ID A0A0M8VBW2_9ACTN Unreviewed; 752 AA.
AC A0A0M8VBW2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=ADL01_30235 {ECO:0000313|EMBL:KOV62224.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV62224.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV62224.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV62224.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-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:KOV62224.1}.
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DR EMBL; LGDW01000447; KOV62224.1; -; Genomic_DNA.
DR RefSeq; WP_053745158.1; NZ_LGDW01000447.1.
DR AlphaFoldDB; A0A0M8VBW2; -.
DR PATRIC; fig|1519490.3.peg.6584; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000037738; 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:UP000037738};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 9..622
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 629..752
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 416
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 417
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 727
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 752 AA; 83004 MW; DAF4E491D91DF9BD CRC64;
MTATVTVGDR ATEAWRGFAG ARWPELIDVR DFIQANYTPY EGDASFLTGA TARTRAVWER
VGALFPEERA RGILDVDTAT PSTITSHEPG WIDRDRELVV GLQTDAPLKR AIMPNGGLRM
VENSLKAYGY EADPFVTKVF GTYRKTHNDG VFDAYTPTMR TARKVGIITG LPDAYGRGRI
IGDYRRVALY GTDRLIEAKR AEKALLDGRP SSEHVIRDRE ELAEQVKALG ELTRMAATYG
CDVSRPAVTA HEAVQWLYLG YLAAVKEQNG AAMSLGRTST FLDVYLQRDL DAGTIDESRA
QELIDDFVIK LRIVRFLRTP EYDALFSGDP TWVTESIGGG GDDGRTLVTR TSFRFLQTLY
NLGPAPEPNL TVLWSPRLPA GFKEFCAQVS IDTSAVQYES DELIRPRNGD DTAIACCVSA
MAVGKEMQFF GARVNLAKAL LYAVNGGRDE MTGDQVTPEM PALTGEYLDF EELSAAYDRV
LDWLARTYVN TLNVIHYMHD KYAYERLEMA LHDHPVHRFM ACGVAGLSVA ADSLSAVRYA
RVKVIRDATG LAVDFVTEGE FPAYGNNDDR ADSLAVGLVE SFMAKVRRHP TYRDAEHTQS
VLTITSNVVY GKHTGNTPDG RRAGQPFAPG ANPMNGRDRH GVAASALSVA KLPYEQARDG
ISLTTTITPE GLGHAPQERA GHLVGILDAY MSSGGFHMNV NVLNREVLED AMEHPEKYPE
LTIRVSGYAV NFVRLTREQQ LDVISRTFHG TL
//
