ID A0A1I2RPD5_9FIRM Unreviewed; 315 AA.
AC A0A1I2RPD5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Putative pyruvate formate lyase activating enzyme {ECO:0000313|EMBL:SFG42368.1};
GN ORFNames=SAMN05216356_10856 {ECO:0000313|EMBL:SFG42368.1};
OS Oribacterium sp. WCC10.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Oribacterium.
OX NCBI_TaxID=1855343 {ECO:0000313|EMBL:SFG42368.1, ECO:0000313|Proteomes:UP000199160};
RN [1] {ECO:0000313|EMBL:SFG42368.1, ECO:0000313|Proteomes:UP000199160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCC10 {ECO:0000313|EMBL:SFG42368.1,
RC ECO:0000313|Proteomes:UP000199160};
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; FOPH01000008; SFG42368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2RPD5; -.
DR STRING; 1855343.SAMN05216356_10856; -.
DR Proteomes; UP000199160; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-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; IPR040085; MJ0674-like.
DR InterPro; IPR016431; Pyrv-formate_lyase-activ_prd.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43075; FORMATE LYASE ACTIVATING ENZYME, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15630)-RELATED; 1.
DR PANTHER; PTHR43075:SF1; FORMATE LYASE ACTIVATING ENZYME, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15630)-RELATED; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004869; PflX_prd; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01099; Uncharacterised_Radical_SAM_Su; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
PE 4: Predicted;
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:SFG42368.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004869-50}; Pyruvate {ECO:0000313|EMBL:SFG42368.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR004869-50}.
FT DOMAIN 74..180
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|Pfam:PF04055"
FT BINDING 78
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 82
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 85
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 315 AA; 35629 MW; CEB62A3E2DEA3B5D CRC64;
MRKRTGKMLI SENDHSTNPL MEHCELCPRK CGAERNAGKK GVCGVSSDIY VARAALHFWE
EPCISGTNGS GAVFFSGCTL KCVFCQNYEL SHGENGKKVS TGRLAEIFLE LEAKGANNIN
LVTPDHYIPE IKESMISARN QGLKIPYVIN CSGYETFELI HELDGLADIY LDDFKYMDSE
KAGRYSGAFD YPERAKESLA EMMCQCPRPM FDEKGIMQKG VIVRHLLMPG MVRNAKAVVD
YVYDNYGDNV YLSLMHQFTP FERLQKYPEI NRKVTHREYE RLIDYAMEKG ITNAFIQDGS
VAKDSFIPDW NGEGV
//
