ID A0A0D7EHN8_RHOPL Unreviewed; 760 AA.
AC A0A0D7EHN8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=OO17_18805 {ECO:0000313|EMBL:KIZ40025.1};
OS Rhodopseudomonas palustris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=1076 {ECO:0000313|EMBL:KIZ40025.1, ECO:0000313|Proteomes:UP000032515};
RN [1] {ECO:0000313|EMBL:KIZ40025.1, ECO:0000313|Proteomes:UP000032515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL398 {ECO:0000313|EMBL:KIZ40025.1,
RC ECO:0000313|Proteomes:UP000032515};
RA Bentzon-Tilia M., Severin I., Hansen L.H., Riemann L.;
RT "Genomics and ecophysiology of heterotrophic nitrogen fixing bacteria
RT isolated from estuarine surface water.";
RL Submitted (NOV-2014) 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:KIZ40025.1}.
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DR EMBL; JXXE01000382; KIZ40025.1; -; Genomic_DNA.
DR RefSeq; WP_044414494.1; NZ_JXXE01000382.1.
DR AlphaFoldDB; A0A0D7EHN8; -.
DR PATRIC; fig|1076.23.peg.4270; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000032515; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 13..630
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 637..760
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT REGION 621..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 209..236
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 424
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 425
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 735
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 760 AA; 84161 MW; D98C4D22C6222FA5 CRC64;
MNMQVQNPVG VETVNAVSSD PWRDFATGVW TREIEVRDFI QANVTPWTGD AGFLAPATER
TKALWAKLTS LLQAERERGG VLDVDTQTFA SIVSHGAGYI DRDLEQIVGL QTDAPLKRAM
MPFGGWRMVK NGLEAYGFKV DPSFEKIFPT LRKTHNDAVF DIYAPDAVRC RKSGIITGLP
DAYGRGRIIG DYRRVALYGV TRLIEDKKAQ GASLELDSLD EAVLRLREEI AEQIRALKEL
VVMAKAYGFD LSKPAANARE AIQWTYFAYL AAVKESNGAA MSLGRVSNFL DIYIARDIAE
GVLDEATAQE LVDHFVMKLR IVRFLRTPEY DTLFSGDPTW VTESIGGMGL DGRPLVTQSS
FRFLHTLETL GPAPEPNLTV LWSENLPQGF KDYCALTSIR TSSIQYESDD LMRPYWGDDY
GIACCVSAMR IGKQMQFFGA RANLAKAMLY AINGGRDELS GEQIGPTFAP VTGDVLDFDE
VTAKLGPMMD WLAKVYVGAL NAIHYCHDKY MYERIEMALH DRDILRTMAC GIAGLSVAAD
SLSAMKHAKV KVIRDARGLA TDFEIEGDYP AFGNNDDRVD EIAIWLVKEF MTRLRKQKTY
RGSVATMSVL TITSNVVYGK KTGNTPDGRK AGEPFAPGAN PMHRRDVKGA VASMASVAKL
PYAHSQDGIS YTFTIVPSAL GAAEADRVTN LNGLLDGYFA QGGHHINVNV FDRATLLHAM
DHPELYPQLT IRVSGYAVNF TKLTREQQLD VISRTFHDLH
//
