ID A0A094JFG5_9GAMM Unreviewed; 760 AA.
AC A0A094JFG5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=HR45_05445 {ECO:0000313|EMBL:KFZ37957.1};
OS Shewanella mangrovi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1515746 {ECO:0000313|EMBL:KFZ37957.1, ECO:0000313|Proteomes:UP000029264};
RN [1] {ECO:0000313|EMBL:KFZ37957.1, ECO:0000313|Proteomes:UP000029264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YQH10 {ECO:0000313|EMBL:KFZ37957.1,
RC ECO:0000313|Proteomes:UP000029264};
RA Liu Y., Zeng R.;
RT "Shewanella sp. YQH10.";
RL Submitted (JUN-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:KFZ37957.1}.
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DR EMBL; JPEO01000003; KFZ37957.1; -; Genomic_DNA.
DR RefSeq; WP_037440497.1; NZ_JPEO01000003.1.
DR AlphaFoldDB; A0A094JFG5; -.
DR STRING; 1515746.HR45_05445; -.
DR eggNOG; COG1882; Bacteria.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000029264; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368075};
KW Glucose metabolism {ECO:0000256|RuleBase:RU368075};
KW Lyase {ECO:0000313|EMBL:KFZ37957.1};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW ECO:0000256|PIRSR:PIRSR000379-2}; Pyruvate {ECO:0000313|EMBL:KFZ37957.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029264};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 6..625
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 632..760
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 735
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 760 AA; 84454 MW; C6B85844E5B0B1AC CRC64;
MTETTDLFQK AWEGFVPGDW KSEVNVRDFI QNNYTPYEGD EAFLAGPTAA TITLWDKVME
GIKLENSTHA PVDFDTDKVS TIDSHDAGYI EKDLETIVGL QTEAPLKRAL LPNGGIRMIE
GSCKAYDRQL DPQLSYIYSD LRKTHNAGVF DVYTPEILAC RKSGVLTGLP DAYGRGRIIG
DYRRIALYGI DYLMKDKYAQ FGSLQAQLEA GEDLQNVIQL REEIAEQHRA LGQMKTMAAK
YGLDISGPAT NAKEAIQWTY FGYLAAVKSQ NGAAMSLGRT SSFLDAYIER DLKNGVITEE
QAQEMIDHFV MKLRMVRFLR TPEYDELFSG DPIWATESIG GMGLDGRTLV TKNSFRFLHT
LYNMGPSPEP NITVLWSEAL PEGFKKYCAK VSIDTSSIQY ENDDLMRPDF ESDDYGIACC
VSPMIIGKQM QFFGARANLA KTLLYTINGG VDEKMKKQVG PKLGAITSEV LDYDEVISRL
DTMMGWLADQ YVTALNVIHY MHDKYSYEAA LMALHDRDVR RTMACGIAGL SIAADSLSAI
KYAKVKPVRD EDGIAVDFEI EGDYPKFGNN DARVDEIACD LVERFMAKIR DKKMYRNAIP
TQSILTITSN VVYGKKTGNT PDGRRAGAPF APGANPMHGR DEKGAVASLT SVAKLPFAHA
QDGISYTFSI VPNALGKDDG ARRGNLAALM DGYFAHKPGH EGGQHLNVNV MNREMLEDAV
ANPDKYPQLT IRVSGYAVRF NSLTPEQQRD VITRTFTKSI
//
