ID Q185U4_CLOD6 Unreviewed; 458 AA.
AC Q185U4;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Thiamine biosynthesis protein ThiH {ECO:0000313|EMBL:CAJ69040.1};
GN Name=thiH {ECO:0000313|EMBL:CAJ69040.1};
GN OrderedLocusNames=CD630_21560 {ECO:0000313|EMBL:CAJ69040.1};
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ69040.1, ECO:0000313|Proteomes:UP000001978};
RN [1] {ECO:0000313|EMBL:CAJ69040.1, ECO:0000313|Proteomes:UP000001978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630 {ECO:0000313|EMBL:CAJ69040.1,
RC ECO:0000313|Proteomes:UP000001978};
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; AM180355; CAJ69040.1; -; Genomic_DNA.
DR RefSeq; WP_003430581.1; NZ_CP010905.2.
DR RefSeq; YP_001088669.1; NC_009089.1.
DR AlphaFoldDB; Q185U4; -.
DR STRING; 272563.CD630_21560; -.
DR EnsemblBacteria; CAJ69040; CAJ69040; CD630_21560.
DR GeneID; 66354551; -.
DR KEGG; cdf:CD630_21560; -.
DR KEGG; pdc:CDIF630_02387; -.
DR PATRIC; fig|272563.120.peg.2276; -.
DR eggNOG; COG0502; Bacteria.
DR OrthoDB; 9801120at2; -.
DR PhylomeDB; Q185U4; -.
DR BioCyc; PDIF272563:G12WB-2313-MONOMER; -.
DR Proteomes; UP000001978; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR GO; GO:0042364; P:water-soluble vitamin biosynthetic process; IEA:UniProt.
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; IPR024007; FeFe-hyd_mat_HydG.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR034428; ThiH/NoCL/HydG-like.
DR NCBIfam; TIGR03955; rSAM_HydG; 1.
DR PANTHER; PTHR43583; 2-IMINOACETATE SYNTHASE; 1.
DR PANTHER; PTHR43583:SF2; BIOTIN AND THIAMIN SYNTHESIS ASSOCIATED DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00319; Fe_hydrogenase_maturase_(HydG; 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 Reference proteome {ECO:0000313|Proteomes:UP000001978};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 262..369
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
SQ SEQUENCE 458 AA; 52173 MW; AEA6A4E642AB8A74 CRC64;
MFINHELINS LLEDAKNSTS DDIEKVLDKA DRREKLSYKD IATLLEVEDK KQLDRLFSIA
GQIKNEIYGN RVVLFAPLYV SNYCVNECVY CGFSKCNKFK RKKLTMEEIK EEVKILEKMG
HKRLALEAGE DPKNCDINYI LDCLDAIYST YNENGNIRRV NVNIAATSVD EYKLLKEKGI
GTYILFQETY HKPTFIKMHG QSIKNDYYYH LTAFDRAMEA GVDDVGAGVL FGLSDPKFEV
LGLMMHNEHL EEKFGVGFHT ISFPRLKKAE GMSLEDFPHL VSDDMFKKIV AITRLAVPFT
GIIMSTRETA EMRNELLKYG VSQISAGSLT GVGGYKAYED GDNTEQFEVG DHRSPVEVLK
ELITDGYIPS YCTACYRKGR TGDRFMSLAK SRQIHNVCTP NALTTLNEFL IDYGDEELKI
MGKKLIAEEI GKIEREDIRN IVSNNMTALE RGERDLYL
//
