ID Y573_CLOBK Reviewed; 643 AA.
AC B1ID91;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=UPF0313 protein CLD_0573 {ECO:0000255|HAMAP-Rule:MF_01251};
GN OrderedLocusNames=CLD_0573;
OS Clostridium botulinum (strain Okra / Type B1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okra / Type B1;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01251};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000255|HAMAP-Rule:MF_01251};
CC -!- SIMILARITY: Belongs to the UPF0313 family. {ECO:0000255|HAMAP-
CC Rule:MF_01251}.
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DR EMBL; CP000939; ACA44151.1; -; Genomic_DNA.
DR AlphaFoldDB; B1ID91; -.
DR KEGG; cbb:CLD_0573; -.
DR HOGENOM; CLU_018288_2_0_9; -.
DR Proteomes; UP000008541; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR HAMAP; MF_01251; UPF0313; 1.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR022946; UPF0313.
DR InterPro; IPR024560; UPF0313_C.
DR InterPro; IPR013704; UPF0313_N.
DR NCBIfam; TIGR03904; SAM_YgiQ; 1.
DR PANTHER; PTHR32331; UPF0313 PROTEIN YGIQ; 1.
DR PANTHER; PTHR32331:SF0; UPF0313 PROTEIN YGIQ; 1.
DR Pfam; PF11842; DUF3362; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF08497; Radical_SAM_N; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01069; UPF0313; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; S-adenosyl-L-methionine.
FT CHAIN 1..643
FT /note="UPF0313 protein CLD_0573"
FT /id="PRO_1000139928"
FT DOMAIN 295..566
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 598..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 309
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01251"
FT BINDING 313
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01251"
FT BINDING 316
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01251"
SQ SEQUENCE 643 AA; 74338 MW; 6715A54A264EC0FD CRC64;
MSNMDFLPIS KEDLKKRNID VLDFIIVTGD AYVDHPSFGT AIIGRVLERE GFTVGIIAQP
NWNNIEDFKK LGKPKYGFLV NSGNIDSMVN HYTASKKKRH DDFYSPGGKS GYRPDRAVIV
YCNKIKEAFK DSPIIIGGIE ASLRRFAHYD YWDNSVRRSI LEDSSADLLI YGMGEKPIVQ
VSNLLRYGMK IDSIKNVRGT TYIEKDIFSL KDYIEIPSFE EVSTNKKSYA EAYKIQYYEQ
DSIRGKTLVQ KHKERYVVQN PPQPPLSQEE MDEVYALPYA RTYHPMYEAE GGIPAIKEVK
FSITSHRGCY GSCSFCALTF HQGRVIQNRS QDSILKEANM MTNMKDFKGY IHDVGGPTAN
FRHRACKVQE KHGTCKNKQC VFPKACKNLI VDHKEYLSLL RKIRKIPNVK KVFIRSGIRF
DYLMYDKNDE FFKELCEHHI SGQLKVAPEH ISDKVLNLMG KPTRNVYDSF VKKYYDINKK
IHKNQFLVPY LMSSHPGSDL KAAIELAQYI KKMGYTPEQV QDFYPTPGSL STTMYYTGIN
PLTEEKVYIP KDQKEKRMQR ALLQFSIHDN YDLVKEALIK AHREDLIGNG PDCLIPYNKP
YKKSHKKNNA KNNNNHYNKN NNKNKDISKK NKKNSLSKHK KRK
//
