ID I8XMR6_9BACE Unreviewed; 252 AA.
AC I8XMR6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Pyruvate formate-lyase-activating enzyme {ECO:0000256|RuleBase:RU362053};
DE EC=1.97.1.4 {ECO:0000256|RuleBase:RU362053};
GN ORFNames=HMPREF1068_01737 {ECO:0000313|EMBL:EIY52190.1};
OS Bacteroides nordii CL02T12C05.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=997884 {ECO:0000313|EMBL:EIY52190.1, ECO:0000313|Proteomes:UP000003089};
RN [1] {ECO:0000313|EMBL:EIY52190.1, ECO:0000313|Proteomes:UP000003089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL02T12C05 {ECO:0000313|EMBL:EIY52190.1,
RC ECO:0000313|Proteomes:UP000003089};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides nordii CL02T12C05.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Activation of pyruvate formate-lyase under anaerobic
CC conditions by generation of an organic free radical, using S-
CC adenosylmethionine and reduced flavodoxin as cosubstrates to produce
CC 5'-deoxy-adenosine. {ECO:0000256|RuleBase:RU362053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-[formate C-acetyltransferase] + reduced [flavodoxin] +
CC S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-
CC [formate C-acetyltransferase] + H(+) + L-methionine + semiquinone
CC [flavodoxin]; Xref=Rhea:RHEA:19225, Rhea:RHEA-COMP:10622, Rhea:RHEA-
CC COMP:12190, Rhea:RHEA-COMP:12191, Rhea:RHEA-COMP:14480,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29947,
CC ChEBI:CHEBI:32722, ChEBI:CHEBI:57618, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:140311; EC=1.97.1.4;
CC Evidence={ECO:0000256|RuleBase:RU362053};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU362053};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|RuleBase:RU362053};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362053}.
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000256|ARBA:ARBA00009777, ECO:0000256|RuleBase:RU362053}.
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:EIY52190.1}.
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DR EMBL; AGXS01000015; EIY52190.1; -; Genomic_DNA.
DR RefSeq; WP_007484768.1; NZ_JH724314.1.
DR AlphaFoldDB; I8XMR6; -.
DR STRING; 997884.HMPREF1068_01737; -.
DR PATRIC; fig|997884.3.peg.1767; -.
DR eggNOG; COG1180; Bacteria.
DR HOGENOM; CLU_058969_1_1_10; -.
DR Proteomes; UP000003089; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR012839; Organic_radical_activase.
DR InterPro; IPR012838; PFL1_activating.
DR InterPro; IPR001989; Radical_activat_CS.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR02493; PFLA; 1.
DR PANTHER; PTHR30352:SF23; PYRUVATE FORMATE-LYASE 1-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000371; PFL_act_enz; 2.
DR SFLD; SFLDG01066; organic_radical-activating_enz; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU362053};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU362053};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362053};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362053};
KW Lyase {ECO:0000313|EMBL:EIY52190.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362053};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362053}; Pyruvate {ECO:0000313|EMBL:EIY52190.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003089};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU362053}.
FT DOMAIN 24..244
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 252 AA; 28951 MW; A32BB3A06FC938B8 CRC64;
MNFQFSTFNF QLIKVHSYES MGTFDGPGLR LVVFLQGCNF RCLYCANPDT IAVKGGTATD
PEEIVRMAIN QKPFFGKRGG ITFSGGEPTL QAEALLPLFH RLKEEGIHIC LDSNGGLWNE
HVEKLLKLTD LVLLDIKEFN LPHHQKLTGR SNEQTLHTAA WLEEHKRPFW LRYVLVPGYS
DFEEDIRAMG QQLGSYQMIQ KVEILPYHTL GVHKYEAMKQ EYLLKGIKEN TPEQIEQAAN
LFKEYFKTVQ IN
//
