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Database: UniProt
Entry: Q5LCA3_BACFN
LinkDB: Q5LCA3_BACFN
Original site: Q5LCA3_BACFN 
ID   Q5LCA3_BACFN            Unreviewed;       374 AA.
AC   Q5LCA3;
DT   21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   21-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Thiazole biosynthesis protein ThiH {ECO:0000313|EMBL:CAH08262.1};
GN   Name=thiH {ECO:0000313|EMBL:CAH08262.1};
GN   ORFNames=BF9343_2481 {ECO:0000313|EMBL:CAH08262.1};
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH08262.1, ECO:0000313|Proteomes:UP000006731};
RN   [1] {ECO:0000313|EMBL:CAH08262.1, ECO:0000313|Proteomes:UP000006731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC   Onslow {ECO:0000313|Proteomes:UP000006731};
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; CR626927; CAH08262.1; -; Genomic_DNA.
DR   RefSeq; WP_005788055.1; NZ_UFTH01000001.1.
DR   PaxDb; 272559-BF9343_2481; -.
DR   GeneID; 66328406; -.
DR   KEGG; bfs:BF9343_2481; -.
DR   eggNOG; COG0502; Bacteria.
DR   HOGENOM; CLU_046249_1_0_10; -.
DR   BioCyc; BFRA272559:G1GHZ-2699-MONOMER; -.
DR   Proteomes; UP000006731; Chromosome.
DR   GO; GO:0036355; F:2-iminoacetate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; 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   Reference proteome {ECO:0000313|Proteomes:UP000006731};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
SQ   SEQUENCE   374 AA;  43010 MW;  1F8B17EC9EE2A0A7 CRC64;
     MFSDELEKIS WEETTKAIYS KTDADVRRAL SKEHCDVNDF MALISPAAAP YLETMARLSR
     KYTMERFGKT ISMFVPLYIT NSCTNSCVYC GFNHNNPMKR TILTEEEMVN EYKAIKKLAP
     FENLLLVTGE NPAKAGVDYI ERALLLAKPY FANLQIEVMP LKAEEYERLT HAGLNGVICF
     QETYNKANYN IYHPRGMKSK FEWRVNGFDR MGQAGVHKIG MGVLIGLEEW RTDITMMAYH
     LRYLQKHYWK TKYSVNFPRM RPSENGGFQP NVVMNDRELA QVTFAMRIFD HDVDISYSTR
     ESAAFRNHMA TLGVTTMSAE SKTEPGGYFT YPQALEQFHV SDERKAVEVD AALRSLGRIP
     VYKDWDTALT LPQC
//
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