ID A0A1G5UYJ3_9FIRM Unreviewed; 278 AA.
AC A0A1G5UYJ3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Pyruvate formate lyase activating enzyme {ECO:0000313|EMBL:SDA38690.1};
GN ORFNames=SAMN02910368_00195 {ECO:0000313|EMBL:SDA38690.1};
OS Lachnospiraceae bacterium G11.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1200747 {ECO:0000313|EMBL:SDA38690.1, ECO:0000313|Proteomes:UP000198652};
RN [1] {ECO:0000313|EMBL:SDA38690.1, ECO:0000313|Proteomes:UP000198652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G11 {ECO:0000313|EMBL:SDA38690.1,
RC ECO:0000313|Proteomes:UP000198652};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRSR:PIRSR004869-50};
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|PIRSR:PIRSR004869-50};
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DR EMBL; FMWZ01000004; SDA38690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5UYJ3; -.
DR STRING; 1200747.SAMN02910368_00195; -.
DR OrthoDB; 9778883at2; -.
DR Proteomes; UP000198652; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR027596; AmmeMemoSam_rS.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR016431; Pyrv-formate_lyase-activ_prd.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR04337; AmmeMemoSam_rS; 1.
DR PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR30352:SF5; TRNA 4-DEMETHYLWYOSINE SYNTHASE (ADOMET-DEPENDENT); 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004869; PflX_prd; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01101; Uncharacterised_Radical_SAM_Su; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR004869-50};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR004869-
KW 50}; Lyase {ECO:0000313|EMBL:SDA38690.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004869-50}; Pyruvate {ECO:0000313|EMBL:SDA38690.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198652};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR004869-50}.
FT DOMAIN 54..277
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR004869-50"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR004869-50"
FT BINDING 76
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR004869-50"
SQ SEQUENCE 278 AA; 31673 MW; BF33D988F8828936 CRC64;
MAKCEVCFRH CEIEEGGRGF CKVRTCKDGV IKPVNYGKVT SLALDPIEKK PLARFKPGSK
ILSLGSYGCN LRCPFCQNHE ISWSDFAYML EKDSEYLSPE ELCRIAIDCK DKGNIGVAFT
YNEPLIDYEY IIDAAKLIHE NDMYVVLVSN GTADVEIAKK LKPYVDAMNI DLKGFTKEFY
RDVLKGDFDS VKAFIEEAVK YAHVELTTLI IPGENDSEEE MREISNYIAG LSDEIPLHIS
RFFPKFHMLD RPATDVKHIY KLADIARQKL KYVYTGNC
//
