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Database: UniProt
Entry: Q65VK2_MANSM
LinkDB: Q65VK2_MANSM
Original site: Q65VK2_MANSM 
ID   Q65VK2_MANSM            Unreviewed;       770 AA.
AC   Q65VK2;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 105.
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   Name=pflD {ECO:0000313|EMBL:AAU37008.1};
GN   OrderedLocusNames=MS0401 {ECO:0000313|EMBL:AAU37008.1};
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988 {ECO:0000313|EMBL:AAU37008.1, ECO:0000313|Proteomes:UP000000607};
RN   [1] {ECO:0000313|EMBL:AAU37008.1, ECO:0000313|Proteomes:UP000000607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E {ECO:0000313|EMBL:AAU37008.1,
RC   ECO:0000313|Proteomes:UP000000607};
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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}.
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DR   EMBL; AE016827; AAU37008.1; -; Genomic_DNA.
DR   RefSeq; WP_011199583.1; NC_006300.1.
DR   AlphaFoldDB; Q65VK2; -.
DR   STRING; 221988.MS0401; -.
DR   KEGG; msu:MS0401; -.
DR   eggNOG; COG1882; Bacteria.
DR   HOGENOM; CLU_023898_0_0_6; -.
DR   OMA; FVIKLRI; -.
DR   OrthoDB; 9803969at2; -.
DR   UniPathway; UPA00920; UER00891.
DR   Proteomes; UP000000607; Chromosome.
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|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          6..635
FT                   /note="PFL"
FT                   /evidence="ECO:0000259|PROSITE:PS51554"
FT   DOMAIN          642..770
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         745
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   770 AA;  86267 MW;  3AA2520528C54BA9 CRC64;
     MAELTEAQKK AWEGFVPGEW QNGVNLRDFI QKNYTPYEGD ESFLADATPA TSELWNSVME
     GIKIENKTHA PLDFDEHTPS TITSHKPGYI NKDLEKIVGL QTDAPLKRAI MPYGGIKMIK
     GSCEVYGRKL DPQVEFIFTE YRKTHNQGVF DVYTPDILRC RKSGVLTGLP DAYGRGRIIG
     DYRRLAVYGI DYLMKDKKAQ FDSLQPRLEA GEDIQATIQL REEIAEQHRA LGKIKEMAAS
     YGYDISGPAT NAQEAIQWTY FAYLAAVKSQ NGAAMSFGRT STFLDIYIER DLKRGLITEQ
     QAQELMDHLV MKLRMVRFLR TPEYDQLFSG DPMWATETIA GMGLDGRPLV TKNSFRVLHT
     LYTMGTSPEP NLTILWSEQL PEAFKRFCAK VSIDTSSVQY ENDDLMRPDF NNDDYAIACC
     VSPMVVGKQM QFFGARANLA KTMLYAINGG IDEKNGMQVG PKTAPITDEV LNFDTVIERM
     DSFMDWLATQ YVTALNIIHF MHDKYAYEAA LMAFHDRDVF RTMACGIAGL SVAADSLSAI
     KYAKVKPIRG DIKDKDGNVV ASNVAIDFEI EGEYPQFGNN DPRVDDLAVD LVERFMKKVQ
     KHKTYRNATP TQSILTITSN VVYGKKTGNT PDGRRAGAPF GPGANPMHGR DQKGAVASLT
     SVAKLPFAYA KDGISYTFSI VPNALGKDDE AQKRNLAGLM DGYFHHEATV EGGQHLNVNV
     LNREMLLDAM ENPEKYPQLT IRVSGYAVRF NSLTKEQQQD VITRTFTQSM
//
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