ID A0A1M4Y036_9BACT Unreviewed; 336 AA.
AC A0A1M4Y036;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Pyruvate formate lyase activating enzyme {ECO:0000313|EMBL:SHE99197.1};
GN ORFNames=SAMN05444274_103186 {ECO:0000313|EMBL:SHE99197.1};
OS Mariniphaga anaerophila.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Mariniphaga.
OX NCBI_TaxID=1484053 {ECO:0000313|EMBL:SHE99197.1, ECO:0000313|Proteomes:UP000184164};
RN [1] {ECO:0000313|EMBL:SHE99197.1, ECO:0000313|Proteomes:UP000184164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26910 {ECO:0000313|EMBL:SHE99197.1,
RC ECO:0000313|Proteomes:UP000184164};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQUM01000003; SHE99197.1; -; Genomic_DNA.
DR RefSeq; WP_073000842.1; NZ_FQUM01000003.1.
DR AlphaFoldDB; A0A1M4Y036; -.
DR STRING; 1484053.SAMN05444274_103186; -.
DR OrthoDB; 9781783at2; -.
DR Proteomes; UP000184164; 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; 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; PF13353; Fer4_12; 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 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:SHE99197.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004869-50}; Pyruvate {ECO:0000313|EMBL:SHE99197.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184164};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR004869-50}.
FT DOMAIN 67..285
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
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 86
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 89
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 336 AA; 37677 MW; F5708E918076326E CRC64;
MQEARFYQKT NGGAIKCLLC PWLCELNPGQ TGVCKVRENI SGTLFTHVYN QVAATGIDPI
EKKPLYHFFP GKNILSIGEV GCNLHCSFCQ NHSISQCSAK QFGGFRKTTP EQLVALALNA
KNNVGVAYTY NEPFTFFEFM FDVARQAKSA GLKNVVVSNG YANPEPLKQL LPFIDAFNID
LKAFDTGFYK QQTKGNLASV LESLKTIAKN GNHLEITNLV IPGLNDDETT FEKMVRWISD
ELGPHVPLHL SRYFPKYKLN LSPTPTEKLE QLFQIANSHL KFVYLGNVND KQHSSTFCTK
CNSLLIERNR YEAKIVQMEF SGTCKICGTP AHIVME
//
