ID A0A101E701_9FIRM Unreviewed; 378 AA.
AC A0A101E701;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Thiazole biosynthesis protein ThiH {ECO:0000313|EMBL:KUK09958.1};
GN ORFNames=XD50_1757 {ECO:0000313|EMBL:KUK09958.1};
OS Clostridia bacterium 41_269.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1635275 {ECO:0000313|EMBL:KUK09958.1, ECO:0000313|Proteomes:UP000053409};
RN [1] {ECO:0000313|Proteomes:UP000053409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(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:KUK09958.1}.
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DR EMBL; LGEZ01000030; KUK09958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101E701; -.
DR STRING; 1635275.XD50_1757; -.
DR PATRIC; fig|1635275.3.peg.706; -.
DR Proteomes; UP000053409; 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; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00876; BATS; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 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 265..369
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
SQ SEQUENCE 378 AA; 43814 MW; D23EDF5A68EA9664 CRC64;
MVKISKTTFY DELVRYRSFY KEMEKEKDRI TPSHIKAVIQ KSYLSPWDYF VLLSEKAEPY
LEDMAQKARR LTIQNFGKVI LLYTPLYLAN YCVNQCSYCG FNVKNKIERT KLTLEEVERE
AKLISSTEMR HILILTGESR IHTPVSYIRD CVRVLRKYFT SISIEVYPME TEEYAELIKE
GVDGLTIYQE VYDEEVYDRV HIAGPKKNFR YRLEAPERAC DAGMRFVNIG ALLGLGDDWR
FEAFFTGLHA YYLQNKYPDS EIGVGLPRLR PHIGAPFKPK PLVSDKNLVQ ILVATRLFLP
RAGISITTRE SEWLRNNLLP LGVTRMSAGS VTAVGGRAVE EKTPGQFEIA DERSVREVHE
YLLKRGYQPV YKDWQAIV
//
