ID B0SS17_LEPBP Unreviewed; 367 AA.
AC B0SS17;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Radical SAM core domain-containing protein {ECO:0000259|PROSITE:PS51918};
GN OrderedLocusNames=LEPBI_I1801 {ECO:0000313|EMBL:ABZ97907.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ97907.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ97907.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP000786; ABZ97907.1; -; Genomic_DNA.
DR RefSeq; WP_012388785.1; NC_010602.1.
DR AlphaFoldDB; B0SS17; -.
DR STRING; 456481.LEPBI_I1801; -.
DR KEGG; lbi:LEPBI_I1801; -.
DR HOGENOM; CLU_040406_1_0_12; -.
DR OrthoDB; 9802027at2; -.
DR BioCyc; LBIF456481:LEPBI_RS08900-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045567; CofH/MnqC-like_C.
DR InterPro; IPR022431; Cyclic_DHFL_synthase_mqnC.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034405; F420.
DR InterPro; IPR020050; FO_synthase_su2.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR00423; CofH family radical SAM protein; 1.
DR NCBIfam; TIGR03699; menaquin_MqnC; 1.
DR PANTHER; PTHR43076; FO SYNTHASE (COFH); 1.
DR PANTHER; PTHR43076:SF1; LIPOYL SYNTHASE 2; 1.
DR Pfam; PF19288; CofH_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004762; CHP00423; 1.
DR SFLD; SFLDF00342; cyclic_dehypoxanthine_futalosi; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001847};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 61..298
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 367 AA; 41665 MW; 2491CBD8CD14C37C CRC64;
MNLASFSLNP NDPVDSVLLK ATEGKRISPK EGLLLYKEGD FLKIQMVARF LREKIRPHSE
ASYTMFRVVN YTNYCNVECS FCSFMDEIGN GKGYVLSKED ILQKMDYAME EGADQMFLQG
GVYPELPFDY YLDVIRTVKA KYPKMHIRAF SPVEVINLET ITGKPLREVL EILKEAGLDS
VPGAGAEILT ERMRQIISPK KATVAEWVRA METCHEVGLK GSANIVFGSE ETEEEVMEHL
QVVRDLQDRT GGFLSFIPWT FQPQTKRFKV RPVPTHEYLK VLGICRIFLD NIQHIETSVM
VLGKGVGQLA LYSGADDISS VVIEENVLRS FGLKTEKEAR KFLKEGGFRP VRRDLNYEEV
PTNLELV
//
