ID A0A494Z213_9BACI Unreviewed; 747 AA.
AC A0A494Z213;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 08-NOV-2023, entry version 16.
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:RKQ16570.1};
GN ORFNames=D8M05_06745 {ECO:0000313|EMBL:RKQ16570.1};
OS Oceanobacillus bengalensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=1435466 {ECO:0000313|EMBL:RKQ16570.1, ECO:0000313|Proteomes:UP000281813};
RN [1] {ECO:0000313|EMBL:RKQ16570.1, ECO:0000313|Proteomes:UP000281813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1K00260 {ECO:0000313|EMBL:RKQ16570.1,
RC ECO:0000313|Proteomes:UP000281813};
RX PubMed=26303283; DOI=10.1007/s10482-015-0573-5;
RA Yongchang O., Xiang W., Wang G.;
RT "Oceanobacillus bengalensis sp. nov., a bacterium isolated from seawater of
RT the Bay of Bengal.";
RL Antonie Van Leeuwenhoek 108:1189-1196(2015).
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:RKQ16570.1}.
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DR EMBL; RBZO01000008; RKQ16570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494Z213; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000281813; 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:UP000281813};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 1..617
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 624..747
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT REGION 609..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 411
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 412
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 722
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 747 AA; 83751 MW; 77E3D55523069623 CRC64;
MTVTAQKKLD FKGGKWQSEI NVRDFIMNNI TPYVGDESFL AGPTKATLDL WNHVMDLTKK
ERENGGVLDM DTKIVSTITS HGPGYLDKAK EKIVGVQTDE PFKRSLQPFG GIRMAVTAAE
SYGFEVDEEV QHIFTNYRKT HNQGVFDAYT PEMRAARSAG VITGLPDAYG RGRIIGDYRR
VALYGVHRLI EDKQEQLASI GENGIMSEDV IRDREEISEQ IRALNELKQL GASYGFDISG
PATNTQEAFQ WLYLGYLAAI KEQNGAAMSL GRVSTFLDIF IERDLKNGSI SEKEVQEIVD
HFVMKLRLVK FSRTPEYNEL YSGDPTWVTE SIGGIAKDGT ALVTKNSFRF LHTLDNLGTA
PEPNLTVLWS EKLPNNFKRY CAKMSIKTSS IQYENDDLMR DKYGDDYGIA CCVSAMEIGK
QMQFFGARVN LAKALLYAIN GGVDEKSLKQ VAPHYAPIIS DYLDYEEVME KYDRMMDWLA
GLYVNTLNVI HFMHDKYSYE RIEMALHDRD VLRTMACGIA GLSVATDSLS AIKYGNVKVL
RNAEGYAVDY EVEGDYPTYG NNDDRADDIA VYLVKSFMNK VKQHKTYRNA IPTQSVLTIT
SNVVYGKKTG NTPDGRRSGA PFAPGANPMH GRDKKGALAS LSSVAKLPYE DSLDGISNTF
SIVPKALGKD EDTRTANLVG MLDGYTMKGG HHLNVNVFDR ETLLDAMDHP EEYPQLTIRV
SGYAVNFIKL TREQQIDVIN RTFHERK
//
