ID A0A2Z2K928_9BACL Unreviewed; 753 AA.
AC A0A2Z2K928;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 Name=pflB {ECO:0000313|EMBL:ASA23166.1};
GN ORFNames=B9T62_21570 {ECO:0000313|EMBL:ASA23166.1};
OS Paenibacillus donghaensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=414771 {ECO:0000313|EMBL:ASA23166.1, ECO:0000313|Proteomes:UP000249890};
RN [1] {ECO:0000313|EMBL:ASA23166.1, ECO:0000313|Proteomes:UP000249890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13049 {ECO:0000313|EMBL:ASA23166.1,
RC ECO:0000313|Proteomes:UP000249890};
RA Jung B.K., Hong S.-J., Shin J.-H.;
RT "Complete genome sequence of Paenibacillus donghaensis KCTC 13049T isolated
RT from East Sea sediment, South Korea.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of pyruvate to formate and acetyl-
CC CoA. {ECO:0000256|ARBA:ARBA00034302}.
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}.
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DR EMBL; CP021780; ASA23166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z2K928; -.
DR KEGG; pdh:B9T62_21570; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000249890; 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|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:UP000249890};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 6..623
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 630..753
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT REGION 614..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 418
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 728
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 753 AA; 84675 MW; E86842CA262C8147 CRC64;
MSVIEKDVQE VKSGWRGFNK GKWARKVNVN DFIEKNILPY LGKEDFLAGA TENTKELWKI
VSEMTKQEIA NGGVLDVDVN TVSTITSHQP GYIDKDKEQI VGVQTDAPFK RSIQPFGGIK
MMIDACKAYG FELPQEIVDL FTNIRKTHNQ GVFDAYTDDM RAARRAGIIT GLPDAYGRGR
IIGDYRRVAL YGIDFLIKEK KQDLKNLEVD SMNEPVIRLR EEVSEQIRAL SELKKMAEMH
GFDISKPANT AKEAFQWVYF GYLAAIKEQN GAAMSLGRVS SFLDIYVERD VAEGTLTEEQ
AQEMVDHFVM KLRIVKFLRT PDYNDLFSGD PTWVTESIGG MSVNGETRVT KNSFRFLHTL
YNLGPAPEPN LTVLWSEKLP EGFKKFCAKV SIETSAIQYE NDDLMRPIYG DDYGIACCVS
AMRIGKQMQF FGARANLAKA LLYAINGGVD EKSGVQVGPE LPRITSEYLD YDEVMQRFNP
MMDWLAKLYM NTLNVIHYMH DKYSYERIEM ALHDRDILRT MACGIAGLSV ATDSLSAIKY
AKVKPIRNEQ GIAIDFEIEG EFPCYGNNDD AVDDIAVDLV ESFMTKIRKN HAYRDALPTQ
SVLTITSNVV YGKKTGTTPD GRKKGEPFAP GANPMHGRDK KGALASLSSV AKLPYEDSLD
GISNTFSIVP KALGKEEEGR KSNLVSMLDG YFNSKGHHLN VNVFAREQLM DAMEHPENYP
QLTIRVSGYA VNFIKLTREQ QMDVITRTFH GAM
//
