ID M9LJS7_PAEPP Unreviewed; 727 AA.
AC M9LJS7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=PPOP_2903 {ECO:0000313|EMBL:GAC43520.1};
OS Paenibacillus popilliae ATCC 14706.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1212764 {ECO:0000313|EMBL:GAC43520.1, ECO:0000313|Proteomes:UP000029453};
RN [1] {ECO:0000313|EMBL:GAC43520.1, ECO:0000313|Proteomes:UP000029453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14706 {ECO:0000313|EMBL:GAC43520.1,
RC ECO:0000313|Proteomes:UP000029453};
RA Iiyama K., Mori K., Mon H., Chieda Y., Lee J.M., Kusakabe T., Tashiro K.,
RA Asano S., Yasunaga-Aoki C., Shimizu S.;
RT "Draft Genome Sequence of Paenibacillus popilliae ATCC 14706T.";
RL Submitted (OCT-2012) 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}.
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:GAC43520.1}.
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DR EMBL; BALG01000222; GAC43520.1; -; Genomic_DNA.
DR AlphaFoldDB; M9LJS7; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000029453; 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:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368075};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526,
KW ECO:0000256|RuleBase:RU368075}; Lyase {ECO:0000313|EMBL:GAC43520.1};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW ECO:0000256|PIRSR:PIRSR000379-2}; Pyruvate {ECO:0000313|EMBL:GAC43520.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029453};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 1..597
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 604..727
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT REGION 588..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..214
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 391
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 392
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 702
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 727 AA; 82040 MW; 060FF60748879255 CRC64;
MDVPNFLENN IQPYHGDESF LVGPTQNTKD LWDIVSQLSK EERERGGVWD VDVHTPSTIT
SHKPGYLDKD KEKVVGVQTD APFRRSIQPF GGIKMMIDAC KAYGFEMPEE IIKMFTDIRK
THNQGVFDAY TSDMRMARKA GIITGLPDAY GRGRIIGDYR RVALYGVDFL IKMKQKDLKD
LEVDVMTDDV IRDREELSEQ IRALQELKQL AEMHGFDISK PAQHAKEAFQ SVYFGYLAAI
KEQNGAAMSL GRVSSFLDIY VERDLEEGTL TEEEAQELVD HFVMKLRIVK FLRTPDYNDL
FSGDPTWVTE SIGGMAVDGS TRVTKNSFRF LHTLYNLGPA PEPNLTVLWS TKLPEAFKKY
CSKVSIETSS IQYENDDLMR PIYGDDYGIA CCVSAMRIGK QMQFFGARAN LAKCLLYAIN
GGKDEKMGVQ VGPELPPITS EVLDYDEVAK RFKQMMEWLA KLYMNTLNVI HYMHDKYSYE
RIEMALHDRE ILRTMACGIA GLSVAADSLS AIKYAKVRPI RNEQGIAVDF ETEGEYPCYG
NNDDRVDSIA IDLVESFMNM IRKHHAYRNA LPTQSVLTIT SNVVYGKKTG TTPDGRKAGE
PFAPGANPMH GRDRKGALAS LSSVAKLPYE HSLDGISNTF SIVPKALGKE LESRKSNLTS
MMDGYFSSKG HHLNVNVFAR EQLLDAMEHP ENYPQLTIRV SGYAVNFIKL TREQQLDVIN
RTFHGSM
//
