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Database: UniProt
Entry: W6N4L0_CLOTY
LinkDB: W6N4L0_CLOTY
Original site: W6N4L0_CLOTY 
ID   W6N4L0_CLOTY            Unreviewed;       369 AA.
AC   W6N4L0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Thiazole biosynthesis protein ThiH {ECO:0000313|EMBL:CDL91121.1};
GN   ORFNames=CTDIVETGP_1191 {ECO:0000313|EMBL:CDL91121.1};
OS   Clostridium tyrobutyricum DIVETGP.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1408889 {ECO:0000313|EMBL:CDL91121.1, ECO:0000313|Proteomes:UP000019482};
RN   [1] {ECO:0000313|EMBL:CDL91121.1, ECO:0000313|Proteomes:UP000019482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DIVETGP {ECO:0000313|EMBL:CDL91121.1,
RC   ECO:0000313|Proteomes:UP000019482};
RA   Soggiu A., Piras C., Gaiarsa S., Sassera D., Roncada P., Bendixen E.,
RA   Brasca M., Bonizzi L.;
RT   "Draft Genome Sequence of Clostridium tyrobutyricum Strain DIVETGP,
RT   Isolated from Cow's Milk for Grana Padano Production.";
RL   Genome Announc. 3:213-215(2015).
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:CDL91121.1}.
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DR   EMBL; CBXI010000019; CDL91121.1; -; Genomic_DNA.
DR   RefSeq; WP_017751011.1; NZ_CBXI010000019.1.
DR   AlphaFoldDB; W6N4L0; -.
DR   GeneID; 29418705; -.
DR   OrthoDB; 9801120at2; -.
DR   Proteomes; UP000019482; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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   CDD; cd01335; Radical_SAM; 1.
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; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00876; BATS; 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};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019482};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          70..299
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   369 AA;  42538 MW;  B1E60B4F7AAF9291 CRC64;
     MGIYEEIHQY DDFDFDSFFN DVTDNQIEKI LLKDRITRED FLALLSPRAE KYIEPMAKKA
     RDITLRNFGK SIVLYTPMYI ANYCTNKCIY CGYNVENKIA RKKMTYEEIE KEAKSIAETG
     LKHIILLTGE SRYHCPMDYL KEAVKILKKY FDSICLEIYP LEEDEYRELV SLGANSLTVY
     QETYNEEVYK SVHLAGKKRD YRYRLEALDR GCRAGIHSVG MSALLGLYKW RNEVFLTGVH
     ADYISRTYPS VEISMSVPRI RPHAGSPIKI YDVTDRNFVQ AAMAYKIFLQ RAGFNVTTRE
     SAKMRNNLIP LGVTKMSAGV TTEVGGHSLN DKDKGEGQFQ ISDGRSVDEI KATVEKLGYN
     PVFKDWQFC
//
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