ID D3S5R4_METSF Unreviewed; 338 AA.
AC D3S5R4;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:ADC70178.1};
GN OrderedLocusNames=MFS40622_1506 {ECO:0000313|EMBL:ADC70178.1};
OS Methanocaldococcus sp. (strain FS406-22).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=644281 {ECO:0000313|EMBL:ADC70178.1, ECO:0000313|Proteomes:UP000002189};
RN [1] {ECO:0000313|EMBL:ADC70178.1, ECO:0000313|Proteomes:UP000002189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS406-22 {ECO:0000313|EMBL:ADC70178.1,
RC ECO:0000313|Proteomes:UP000002189};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Leigh J.,
RA Whitman W.B., Woyke T.;
RT "Complete sequence of chromosome of Methanocaldococcus sp. FS406-22.";
RL Submitted (FEB-2010) 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; CP001901; ADC70178.1; -; Genomic_DNA.
DR AlphaFoldDB; D3S5R4; -.
DR STRING; 644281.MFS40622_1506; -.
DR KEGG; mfs:MFS40622_1506; -.
DR eggNOG; arCOG00934; Archaea.
DR HOGENOM; CLU_062674_0_1_2; -.
DR OMA; WNSNMYM; -.
DR OrthoDB; 371936at2157; -.
DR Proteomes; UP000002189; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; 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.
DR PROSITE; PS51918; RADICAL_SAM; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004869-50};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR004869-50}.
FT DOMAIN 111..334
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 129
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 133
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 136
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 338 AA; 40151 MW; DE6BF408CE284F53 CRC64;
MKLSRYLAIS RDLAPAKFMI AKCIEVEEFN GLELNELWEI HNKILKKVDF DDFDFNNLEF
VKPNLLDLKV EIAKRIFRNC HFCEHRCYAN REFERGFCRI KESYYSTEFL HLGEERVLVP
SHTIFFCGCN FKCVFCQNWD ISQVYFDTTI PNHCIPYNPK EMAKIIKHKR DYSKNVNFVG
GDPTPHLLSI LKTLNYLDKN IPVVWNSNMY LTVKGMYLLK GVVDVYLTDF KFGNNECGER
LSKVKNYFDI VGRNHLLIKD EEVIIRHLVM PNHLDCCTER IFDFISKNLD NAVVNVMFQY
RPEYKAKEYP DINRRLTYDE IEKALELAEE YKLDLIYD
//