ID H3NER1_9LACT Unreviewed; 749 AA.
AC H3NER1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=HMPREF9703_01042 {ECO:0000313|EMBL:EHR32926.1};
OS Dolosigranulum pigrum ATCC 51524.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Dolosigranulum.
OX NCBI_TaxID=883103 {ECO:0000313|EMBL:EHR32926.1, ECO:0000313|Proteomes:UP000003599};
RN [1] {ECO:0000313|EMBL:EHR32926.1, ECO:0000313|Proteomes:UP000003599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51524 {ECO:0000313|EMBL:EHR32926.1,
RC ECO:0000313|Proteomes:UP000003599};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dolosigranulum pigrum ATCC 51524.";
RL Submitted (JAN-2012) 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|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:EHR32926.1}.
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DR EMBL; AGEF01000009; EHR32926.1; -; Genomic_DNA.
DR AlphaFoldDB; H3NER1; -.
DR STRING; 29394.BWX42_03145; -.
DR PATRIC; fig|883103.3.peg.1015; -.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_023898_0_0_9; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000003599; 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:UP000003599};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 3..619
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 626..749
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 413
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 414
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 724
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 749 AA; 84386 MW; 43D9DA0303830FEE CRC64;
MNTKVADIKQ WDGFKEGKWQ ESVDVRDFIQ NNYDLYEGDE SFLAEATDAT KQLWEQVMEL
NRKEFAAGGV LDMDTEVVST ITSHGAAYLN KELETIVGFQ TDKPFKRSFQ PFGGIRMAEL
SAEAYGYEID SEMSHIFRDY RKTHNDGVFS AYTPEMREVR RSGVITGLPD AYGRGRIIGD
YRRVALYGLD FLIEDKKREH STYGNGKMTE AVIRQREELS EQIKSLNELI ELGRIYGYDL
SRPAETAQEA FQWTYLAYLA AIKQQNGAAM SLGRVSTFLD IYIERDLERG VITEKEAQEF
VDHFVMKLRL VKFARTPEYN ELFSGDPTWV TEAIAGVGLD GRPLVTKNSF RFLHTLTNLG
PAPEPNLTVL WSPDLPQNFK EYSAKVSIES SAVQYENDEV MRPEYGDDYG IACCVSAMEI
GKQMQFFGAR ANLGKALLYA INGGVDEKSE VQVGPDFGKI ESDILDFDEV MEKYDQVLEW
LCELYINTLN VIHYMHDKYS YESIMMALHD TEIHRTMATG IAGFSVAADA LSAIKYAKVH
VIRNEDGLAV DYKVEGDFPK YGNNDKRVDD LAVDILDRFI TKLKKHDTYR AQETTTSILT
ITSNVVYGKK TGNTPDGRRA GEPFAPGANP LHGRDCQGAL ASLNSVAKLP YKNGKDGISN
TFSIVPGALG KDIDTQKQNL SLMLDGYAKK GGHHLNVNVL NKETLLDAME NPSEYPQLTI
RVSGYAVNFI KLTREQQMDV ISRTFHESM
//
