ID A0A1H9RME4_9BACI Unreviewed; 750 AA.
AC A0A1H9RME4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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 ORFNames=SAMN05444126_10515 {ECO:0000313|EMBL:SER73817.1};
OS Salisediminibacterium haloalkalitolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=1464123 {ECO:0000313|EMBL:SER73817.1, ECO:0000313|Proteomes:UP000199318};
RN [1] {ECO:0000313|EMBL:SER73817.1, ECO:0000313|Proteomes:UP000199318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10nlg {ECO:0000313|EMBL:SER73817.1,
RC ECO:0000313|Proteomes:UP000199318};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOGV01000005; SER73817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9RME4; -.
DR STRING; 1464123.SAMN05444126_10515; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000199318; 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|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:UP000199318};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 6..620
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 627..750
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT REGION 612..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 414
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 415
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 725
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 750 AA; 84514 MW; E271791A059BA1E5 CRC64;
MAMEMESIQK TAWQGFENGD WQHTINVRDF IQKNFRLYDG DESFLAGPTQ ATENLWDKVM
ELTEKERENG GVYDLDTTIV SSITSHGPGY LNQDLEKVVG VQTDVPFKRG LMPYGGIRMA
HNALESYGYT MAAETDEVFK KHRKTHNQGV FDAYTPEMKL ARKVGIITGL PDAYGRGRII
GDYRRVALYG TDQLISAKQA ELNQVTGKMS AETIQLREEI QEQTRALQEL TELGKMYGFD
LSRPAETALE AFQWLYLGYL AAIKEQNGAA MSLGRVSTFL DIYIERDLEN GRLTEEEAQE
LVDHFVMKLR LVKFARTPEY NELFSGDPTW VTESIAGIGE DGRPLVTKSS FRFLHTLSNL
GPAPEPNLTV LWSPKLTDNF KHYCAKMSMD TSSIQYENDE IMRPEYGDDY GIACCVSAME
IGKQMQFFGA RANLAKSLLY AINGGVDEKM NMQVVDGIEP ITSEYLDYDE VSEKFETVMD
WLAELYINTL NIIHYMHDKY SYERIMMALH DKDVRRTMAT GIAGLSVAAD SLSAIKHSNV
RVIRDENGLA VDFEIEGEYP QYGNDDDRVD LIAKSLVEKF SAMLKKHDTY RNAETTMSIL
TITSNVVYGK KTGNTPDGRK DGEPFAPGAN PMHGRDQRGA LASLNSVAKM PYDQALDGIS
NTFSIVPKAL GKDDLTKKAN LSAILDGYMD QTGHHLNVNV FDRETLIDAM DQPEKYPQLT
VRVSGYAVNF IKLTREQQLD VINRTFHETI
//
