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
//