ID D8IFS2_BRAP9 Unreviewed; 474 AA.
AC D8IFS2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Thiamine biosynthesis protein {ECO:0000313|EMBL:ADK31995.1};
GN Name=thiH {ECO:0000313|EMBL:ADK31995.1};
GN OrderedLocusNames=BP951000_2017 {ECO:0000313|EMBL:ADK31995.1};
OS Brachyspira pilosicoli (strain ATCC BAA-1826 / 95/1000).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=759914 {ECO:0000313|EMBL:ADK31995.1, ECO:0000313|Proteomes:UP000000332};
RN [1] {ECO:0000313|EMBL:ADK31995.1, ECO:0000313|Proteomes:UP000000332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1826 / 95/1000 {ECO:0000313|Proteomes:UP000000332};
RX PubMed=20625514; DOI=10.1371/journal.pone.0011455;
RA Wanchanthuek P., Bellgard M.I., La T., Ryan K., Moolhuijzen P., Chapman B.,
RA Black M., Schibeci D., Hunter A., Barrero R., Phillips N.D., Hampson D.J.;
RT "The complete genome sequence of the pathogenic intestinal spirochete
RT Brachyspira pilosicoli and comparison with other Brachyspira genomes.";
RL PLoS ONE 5:E11455-E11455(2010).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP002025; ADK31995.1; -; Genomic_DNA.
DR RefSeq; WP_013244944.1; NC_014330.1.
DR AlphaFoldDB; D8IFS2; -.
DR STRING; 759914.BP951000_2017; -.
DR GeneID; 56440572; -.
DR KEGG; bpo:BP951000_2017; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_046249_0_0_12; -.
DR InParanoid; D8IFS2; -.
DR Proteomes; UP000000332; 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; SFLDG01081; cleavage_of_the_Ca-Cb_bond_in; 1.
DR SFLD; SFLDF00319; Fe_hydrogenase_maturase_(HydG; 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:UP000000332};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 279..385
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
SQ SEQUENCE 474 AA; 53965 MW; 760E237AFF773879 CRC64;
MSSETLFKYD SKSKNANEFI NDEEILKTIS QVESGNYNIR DILNKANEMK GLEPNEALAL
LLCDDKKIEN EMFEIAKKIK LEIYGKRIVL FAPLYLSNYC INGCVYCPYH AKNKHIARKQ
LTQDEIRAEV IALQDMGHKR LALETGEDPD YASMEYLLES IKTIYSIKHK NGAIRRVNVN
IAATTVENYR KLKDAGIGTY VLFQETYHKP TYEKVHPSGP KSNYEYHTEA MDRAMEGGID
DVGIGVLFGL YNYKYDFTAM LYHAKHLEET FGCGPHTISV PRIRPADDVD VKSFPNAITD
SLFKKIVAVL RIAVPYTGII VSTRESQKSR EEALEVGVSQ ISGGSRTSVG GYVEEEEENS
KQFEISDNRS LDDIIKWLCD IDYLPSFCTA CYREGRTGDR FMSFAKSGQI KNFCQANAII
TLKEYENDYA KEETKKSIDK VMNNEIERIP NEKVKAKLVE ALKGIDEGKR DFKF
//
