ID A0A1M4M934_9FIRM Unreviewed; 472 AA.
AC A0A1M4M934;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Thiazole biosynthesis protein thiH {ECO:0000313|EMBL:SCG84198.1};
GN Name=thiH {ECO:0000313|EMBL:SCG84198.1};
GN ORFNames=DW1_2638 {ECO:0000313|EMBL:SCG84198.1};
OS Proteiniborus sp. DW1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Proteiniborus.
OX NCBI_TaxID=1889883 {ECO:0000313|EMBL:SCG84198.1, ECO:0000313|Proteomes:UP000185208};
RN [1] {ECO:0000313|EMBL:SCG84198.1, ECO:0000313|Proteomes:UP000185208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW1 {ECO:0000313|EMBL:SCG84198.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; FMDO01000054; SCG84198.1; -; Genomic_DNA.
DR RefSeq; WP_074351157.1; NZ_FMDO01000054.1.
DR AlphaFoldDB; A0A1M4M934; -.
DR STRING; 1889883.DW1_2638; -.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000185208; 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: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:UP000185208};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 275..383
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
SQ SEQUENCE 472 AA; 53747 MW; C657E29763E9C7A6 CRC64;
MYNPKSLRAE EFISHEEVSE TLEYAQRNKN NMELIDSIIG KAKLRRGLNH REASVLLACE
IPEKISEIYA LAEQIKRDIY GNRIVLFAPL YLSNYCINGC VYCPYHLKNK HIARKKLTQE
DIIREVVALM DMGHKRLAIE AGEHPSINPI EYILESIDTI YSIKHKNGAI RRVNVNIAAT
TVENYRKLKE AGIGTYILFQ ETYHKESYEK LHPTGPKHDY AYHTEAMDRA MEGGIDDVGL
GVLFGLELYK YEFAALLMHA EHLEAVYGVG PHTISVPRIK PADDIDPSAF DNSISDEIFA
KICACIRISV PYTGMIISTR ESQAVREKVI RLGVSQISGA SKTSVGGYCE PEPENEKSEQ
FEISDRRTLD EVVRWLMEKG YIPSFCTACY REGRTGDRFM SLSKSGQIQN CCHPNALMTL
KEYIEDYASS ETKLIGEKVI QKEIENIPND KVKRIVHENL INIKNGQRDF RL
//
