ID R7D164_9BACE Unreviewed; 377 AA.
AC R7D164;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Thiazole biosynthesis protein ThiH {ECO:0000313|EMBL:CDD83527.1};
GN ORFNames=BN666_02807 {ECO:0000313|EMBL:CDD83527.1};
OS Bacteroides sp. CAG:462.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262740 {ECO:0000313|EMBL:CDD83527.1, ECO:0000313|Proteomes:UP000018063};
RN [1] {ECO:0000313|EMBL:CDD83527.1, ECO:0000313|Proteomes:UP000018063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:462 {ECO:0000313|Proteomes:UP000018063};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDD83527.1}.
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DR EMBL; CBHU010000188; CDD83527.1; -; Genomic_DNA.
DR AlphaFoldDB; R7D164; -.
DR STRING; 1262740.BN666_02807; -.
DR Proteomes; UP000018063; 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 Reference proteome {ECO:0000313|Proteomes:UP000018063};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 69..298
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 377 AA; 43421 MW; 993766A6C6A9F7A2 CRC64;
MFSDELEKIS WDETTKKILS KTDADVRRAL SKEHCDVEDF MALISPAAEP YLETMARLSQ
KYTLERFGKT ISMFVPLYIT NSCTNSCIYC GFHASNPMKR TILTEEEMVN EYKAIKKLAP
FENLLIVTGE NPAKAGVPYI ARALDLAKPY FSNLKIEVMP LSAEEYEELT HHGLNGVICF
QETYNKANYK IYHPRGMKSN FEWRVNGFDR MGQAGVHSIG MGVLIGLEDW RTDVTMMAYH
LRYLQKHYWK TKYSVNFPRM RPSENGGFQP NVIMSDRELA QLTFAMRIFD HDVDISYSTR
ESAEFRDHMA TLGVTTMSAE SKTEPGGYYS YPQTLEQFHV SDERKAVEVW KALQRLGREP
VWKDWDASFD ATRAAGR
//
