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Database: UniProt
Entry: E1J1M4_ECOLX
LinkDB: E1J1M4_ECOLX
Original site: E1J1M4_ECOLX 
ID   E1J1M4_ECOLX            Unreviewed;       377 AA.
AC   E1J1M4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Thiazole biosynthesis protein ThiH {ECO:0000313|EMBL:EFK70121.1};
GN   Name=thiH {ECO:0000313|EMBL:EFK70121.1};
GN   ORFNames=HMPREF9347_00772 {ECO:0000313|EMBL:EFK70121.1};
OS   Escherichia coli MS 124-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=679205 {ECO:0000313|EMBL:EFK70121.1, ECO:0000313|Proteomes:UP000003390};
RN   [1] {ECO:0000313|EMBL:EFK70121.1, ECO:0000313|Proteomes:UP000003390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS 124-1 {ECO:0000313|EMBL:EFK70121.1,
RC   ECO:0000313|Proteomes:UP000003390};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (JUL-2010) 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:EFK70121.1}.
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DR   EMBL; ADWT01000004; EFK70121.1; -; Genomic_DNA.
DR   RefSeq; WP_000847461.1; NZ_ADWT01000004.1.
DR   AlphaFoldDB; E1J1M4; -.
DR   Proteomes; UP000003390; 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   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; SFLDG01060; BATS_domain_containing; 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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          71..301
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   377 AA;  43398 MW;  C630426D530E3070 CRC64;
     MKTFSDRWRQ LDWDDIRLRI NGKTAVDVER ALNASQFTRD DMMALLSPAA SGYLEQLAQR
     AQRLTRQRFG NTVSFYVPLY LSNLCANDCT YCGFSMSNRI KRKTLDEADI ARESAAIREM
     GFEHLLLVTG EHQAKVGMDY FRRHLPALRE QFSSLQMEVQ PLAETEYAEL KQLGLDGVMV
     YQETYHEATY ARHHLKGKKQ DFFWRLETPD RLGRAGIDKI GLGALIGLSD NWRVDCYMVA
     EHLLWLQQHY WQSRYSVSFP RLRPCTGGIE PASIMDERQL VQTICAFRLL APEIELSLST
     RESPWFRDRV IPLAINNVSA FSKTQPGGYA DNHPELEQFS PHDDRRPEAV AAALTAQGLQ
     PVWKDWDSYL GRASQRL
//
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