ID B9DVL5_STRU0 Unreviewed; 775 AA.
AC B9DVL5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=pfl {ECO:0000313|EMBL:CAR43361.1};
GN Synonyms=pflB {ECO:0000313|EMBL:CAR43361.1};
GN OrderedLocusNames=SUB1568 {ECO:0000313|EMBL:CAR43361.1};
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495 {ECO:0000313|EMBL:CAR43361.1, ECO:0000313|Proteomes:UP000000449};
RN [1] {ECO:0000313|Proteomes:UP000000449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J {ECO:0000313|Proteomes:UP000000449};
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
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; AM946015; CAR43361.1; -; Genomic_DNA.
DR RefSeq; WP_015911874.1; NC_012004.1.
DR AlphaFoldDB; B9DVL5; -.
DR STRING; 218495.SUB1568; -.
DR KEGG; sub:SUB1568; -.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_023898_0_0_9; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000000449; 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 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:SF8; FORMATE ACETYLTRANSFERASE; 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:UP000000449};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 9..625
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 643..763
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 738
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 775 AA; 87433 MW; 1565718F518ABD0E CRC64;
MATVKTNTDV FEKAWEGFKG TDWKEKASVS RFVQANYTPY DGDESFLAGA TERSLKIKKI
IEETKAGYEA TRFPFDTRPS SIADIPAGYI DKENELIYGI QNDELFKLNF MPKGGIRMAE
TTLKENGYEP DPAVHEIFTK YVTTVNDGIF RAYTSNIRRA RHAHTVTGLP DAYSRGRIIG
VYARLALYGA DYLMQEKVND WNAITEIDEE SIRLREEINL QYQALGEVAK LGDLYGLDVR
RPAENVKEAI QWVNIAFMAV CRVINGAATS LGRVPIVLDI YAERDLARGT FTESEIQEFV
DDFVLKLRTV KFGRTKAYDA LYSGDPTFIT TSMAGMGNDG RHRVTKMDYR FLNTLDTIGN
SPEPNLTVLW TDQLPYAFRR YCMKMSHKHS SIQYEGVTTM AKEGYGEMSC ISCCVSPLDP
ENEEQRHNIQ YFGARVNVLK ALLTGLNGGY DDVHRDYKVF NVVEPITSEI LDYDEVMANF
EKSLDWLTDT YVDALNIIHY MTDKYNYEAV QMAFLPSHQR ANMGFGICGF ANTVDTLSAI
KYATVKTIRD ENGYIYDYEV TGDFPRYGED DDRVDDIAKW LMEAYHTRLA SHKLYKNAEA
SVSLLTITSN VAYSKQTGNS PVHRGVYLNE DGTVNTSKVE FFSPGANPSN KAKGGWLQNL
NSLAKLEFSH ANDGISLTTQ VSPRALGKTF DEQVDNLVTV LDGYFENGGQ HVNLNVMDLN
EVYDKIMSGE DVIVRISGYC VNTKYLTPEQ KQELTQRVFH EVLSMDDAAE AISGK
//
