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Database: UniProt
Entry: C4IFI8_CLOBU
LinkDB: C4IFI8_CLOBU
Original site: C4IFI8_CLOBU 
ID   C4IFI8_CLOBU            Unreviewed;       385 AA.
AC   C4IFI8;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Thiazole biosynthesis protein ThiH {ECO:0000313|EMBL:EEP54321.1};
GN   Name=thiH {ECO:0000313|EMBL:EEP54321.1};
GN   ORFNames=CLP_1692 {ECO:0000313|EMBL:EEP54321.1};
OS   Clostridium butyricum E4 str. BoNT E BL5262.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP54321.1, ECO:0000313|Proteomes:UP000003081};
RN   [1] {ECO:0000313|EMBL:EEP54321.1, ECO:0000313|Proteomes:UP000003081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081};
RA   Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C.,
RA   Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEP54321.1}.
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DR   EMBL; ACOM01000005; EEP54321.1; -; Genomic_DNA.
DR   RefSeq; WP_003411197.1; NZ_ACOM01000005.1.
DR   AlphaFoldDB; C4IFI8; -.
DR   STRING; 1492.ATN24_11565; -.
DR   eggNOG; COG0502; Bacteria.
DR   HOGENOM; CLU_046249_1_0_9; -.
DR   Proteomes; UP000003081; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR010722; BATS_dom.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR012726; ThiH.
DR   InterPro; IPR034428; ThiH/NoCL/HydG-like.
DR   NCBIfam; TIGR02351; thiH; 1.
DR   PANTHER; PTHR43583; 2-IMINOACETATE SYNTHASE; 1.
DR   PANTHER; PTHR43583:SF1; 2-IMINOACETATE SYNTHASE; 1.
DR   Pfam; PF06968; BATS; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDF00301; 2-iminoacetate_synthase_(ThiH); 1.
DR   SFLD; SFLDG01081; cleavage_of_the_Ca-Cb_bond_in; 1.
DR   SMART; SM00876; BATS; 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:UP000003081};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          86..303
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   385 AA;  44046 MW;  207010E07072DA3C CRC64;
     MEQRIDHMKY LPNMEVLEES NIMNEVITRM NSYDYENYTS EDVMTALNKD VLNPEDFAAL
     LSPAAFPFLE QMAQRAKIET RKHFGNSINM FTPLYIANYC ENYCIYCGFN CHNKIKRARL
     NAEEIEKEMQ VIAETGLQEI LLLTGESRSM SDVKYIGEAC KIAKKYFKVI GVEVYPMNSD
     EYAYLHECGV DYVTVFQETY NSDKYETLHL AGHKRIFPYR LNAQERALKG GMRGVGFAAL
     LGLDDFRKDA FATGMHAYLL QKKYPHAEIA FSCPRLRPII NNDNINPKDV HEPQLLQVMC
     AYRIFMPYAA MTISTREQAH FRDNVIGLAA TKISAGVSVG IGGHASEEEK GDEQFEISDP
     RNVDEVYNAI INHDLQPVMS DYVYV
//
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