ID M4YPN2_THEXX Unreviewed; 337 AA.
AC M4YPN2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Pyruvate-formate lyase-activating enzyme {ECO:0000313|EMBL:AGI48372.1};
DE EC=1.97.1.4 {ECO:0000313|EMBL:AGI48372.1};
GN ORFNames=TALC_01394 {ECO:0000313|EMBL:AGI48372.1};
OS Thermoplasmatales archaeon (strain BRNA1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales.
OX NCBI_TaxID=1054217 {ECO:0000313|EMBL:AGI48372.1, ECO:0000313|Proteomes:UP000012076};
RN [1] {ECO:0000313|EMBL:AGI48372.1, ECO:0000313|Proteomes:UP000012076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRNA1 {ECO:0000313|EMBL:AGI48372.1,
RC ECO:0000313|Proteomes:UP000012076};
RA Denman S.E., Evans P., Bragg L., Padmanahba J., McKenzie M., Edwards D.,
RA Krzycki J., McSweeney C., Morrison M.;
RT "Thermoplasmatales-like gut symbionts are pyrrolysine dependent-
RT methanogens.";
RL Submitted (JUL-2011) 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; CP002916; AGI48372.1; -; Genomic_DNA.
DR AlphaFoldDB; M4YPN2; -.
DR STRING; 1054217.TALC_01394; -.
DR KEGG; tar:TALC_01394; -.
DR PATRIC; fig|1054217.5.peg.1325; -.
DR eggNOG; arCOG00946; Archaea.
DR HOGENOM; CLU_044176_1_0_2; -.
DR OMA; YHFYPGS; -.
DR Proteomes; UP000012076; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:UniProtKB-EC.
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:SF5; PYRUVATE FORMATE-LYASE 1-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 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:AGI48372.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004869-50};
KW Oxidoreductase {ECO:0000313|EMBL:AGI48372.1};
KW Pyruvate {ECO:0000313|EMBL:AGI48372.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012076};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR004869-50}.
FT DOMAIN 72..284
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 87
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 91
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 94
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 337 AA; 38299 MW; 76224BEB369E683F CRC64;
MAFINPNHPA KYWHSEGTDC VCDLCPHHCR IKKDGFGLCN SRKNVEGRLV AYNYGRISSI
AVDPIEKKPL YHYYPATSVF SVGGIGCNLR CQYCQNYPIS MDAFGKKRTT YKSPEDIVAL
CRQQKFGRIA FTYNEPSIWY EYIMDVMEED PDLDLVLVTN GMIEEEPLRD LCKVTGAMNI
DVKAFNESFY SKLCGGKLEY VKKTCEIVHA SKVHLELTYL VIPGYNDDED DILEFVKWVR
DSLSPDVPVH FNRFHPDYNM MTVPMTPAET LLRCKEIAED NGLNYAYVGN ILADDATDTY
CPECGASVIK RTGYSVSILG LDGDRCAFCK HKLNIVR
//