ID A0A1T5L8V6_9MICO Unreviewed; 756 AA.
AC A0A1T5L8V6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN04324258_3166 {ECO:0000313|EMBL:SKC72466.1};
OS Krasilnikoviella flava.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Krasilnikoviella.
OX NCBI_TaxID=526729 {ECO:0000313|EMBL:SKC72466.1, ECO:0000313|Proteomes:UP000189777};
RN [1] {ECO:0000313|EMBL:SKC72466.1, ECO:0000313|Proteomes:UP000189777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21481 {ECO:0000313|EMBL:SKC72466.1,
RC ECO:0000313|Proteomes:UP000189777};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUZQ01000005; SKC72466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5L8V6; -.
DR STRING; 526729.SAMN04324258_3166; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000189777; 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:UP000189777};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 6..626
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 633..756
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 731
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 756 AA; 83073 MW; EC18D60EB1BC8024 CRC64;
MTIDTARTTT AGDTTAAWQG FTPGPWCDEI DLRDFIQRNY TPYTGDDSFL AGPTERTTGV
WAKLSAMFPA ERERGVYDVD PHTPAGITAH GPGYIDEDAE LVVGLQTDAP LKRAIMPNGG
WRMVEGALKT YGYPVDENLR KVFTEYRKTH NQGVFDVYPP AVRAARSSHI ITGLPDAYGR
GRIIGDYRRV ALYGVDALVA AKKVDKLGLD VQPFGESVAR EREEHAEQIR ALGELKEMAA
SYGYDISGPA TTAREAVQWL YFGYLAAVKE QNGAAMSLGR TSTFLDVFIE RDLAAGRLTE
PEAQEIVDDF VIKLRIVRFL RTPEYDALFS GDPTWVTETI GGMGEDGRPL VTKNSFRFLQ
TLYNLGPAPE PNMTVFWSPR LPRGFKDFCA KVSIDTSAVQ YESDEQIRPA WGDDAAIACC
VSPMAVGKQM QFFGARVNLA KALLYAINGG KDEVTGKQVS PAFPAVAPGL PLDYDDVRAR
FDRTMDWLAE TYVEALNCIH WSHDKYAYER LEMALHDRDV LRTMACGIAG LSVAADSLSA
IRYATVIPVA DERGIVVDYE TDGDWPAYGN DDDRVDAIAV ELVESFMAKI RSHKMYRDAV
PTQSVLTITS NVVYGKATGN TPDGRRAGEP FSPGANPMNG RDTHGMLASA LSVAKLPYDQ
AQDGISLTNT VVPSGLGRTR EEQVANLAGL LDASVGSGGY HMNVNVLVRE TLEDAMEHPE
KYPQLTIRVS GYAVNFVRLT REQQLDVLSR TFHGGL
//
