ID I5AUB8_EUBCE Unreviewed; 244 AA.
AC I5AUB8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Pyruvate formate-lyase-activating enzyme {ECO:0000256|ARBA:ARBA00021356, ECO:0000256|RuleBase:RU362053};
DE EC=1.97.1.4 {ECO:0000256|RuleBase:RU362053};
GN ORFNames=EubceDRAFT1_1602 {ECO:0000313|EMBL:EIM57391.1};
OS [Eubacterium] cellulosolvens 6.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=633697 {ECO:0000313|EMBL:EIM57391.1, ECO:0000313|Proteomes:UP000005753};
RN [1] {ECO:0000313|EMBL:EIM57391.1, ECO:0000313|Proteomes:UP000005753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6 {ECO:0000313|EMBL:EIM57391.1,
RC ECO:0000313|Proteomes:UP000005753};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Anderson I.J., Johnson E.,
RA Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EIM57391.1, ECO:0000313|Proteomes:UP000005753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6 {ECO:0000313|EMBL:EIM57391.1,
RC ECO:0000313|Proteomes:UP000005753};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Johnson E., Mukhopadhyay B.,
RA Anderson I., Woyke T.;
RT "Improved High-Quality Draft sequence of Eubacterium cellulosolvens 6.";
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|ARBA:ARBA00003141,
CC 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}.
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DR EMBL; CM001487; EIM57391.1; -; Genomic_DNA.
DR AlphaFoldDB; I5AUB8; -.
DR STRING; 633697.EubceDRAFT1_1602; -.
DR eggNOG; COG1180; Bacteria.
DR HOGENOM; CLU_058969_1_1_9; -.
DR OrthoDB; 9782387at2; -.
DR Proteomes; UP000005753; Chromosome.
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; 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 SFLD; SFLDG01066; organic_radical-activating_enz; 1.
DR SFLD; SFLDS00029; Radical_SAM; 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:EIM57391.1};
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:EIM57391.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005753};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU362053}.
FT DOMAIN 15..242
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 244 AA; 28372 MW; EDCAF01557814FDE CRC64;
MIKGAIHSIE TFGSVDGPGV RFVIFVRGCK MRCRYCHNAD TWKMQTDNMK TADELLDQAE
RYKAYWRDDG GITVSGGEPL LQIDFLLDLF KKAKERGIKT CIDTAGQPFT REEPFFSKFK
ELMQYTDLLL VDIKHIDSEE HKKLTAQPNE NIHDMFRYLS EIDKPIWIRH VLVPGITDDD
RWLRETRKFI ETLHNVQRIE VLPYHSLGEF KWEELGVPYT LGGVNPPDAD RVKNAVEILR
GEKE
//
