ID A0A3Q9HQ97_9FIRM Unreviewed; 367 AA.
AC A0A3Q9HQ97;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Thiamine biosynthesis protein ThiH {ECO:0000313|EMBL:AZR73196.1};
GN ORFNames=BBF96_07240 {ECO:0000313|EMBL:AZR73196.1};
OS Anoxybacter fermentans.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Anoxybacter.
OX NCBI_TaxID=1323375 {ECO:0000313|EMBL:AZR73196.1, ECO:0000313|Proteomes:UP000267250};
RN [1] {ECO:0000313|EMBL:AZR73196.1, ECO:0000313|Proteomes:UP000267250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY22613 {ECO:0000313|EMBL:AZR73196.1,
RC ECO:0000313|Proteomes:UP000267250};
RA Zeng X., Shao Z.;
RT "Genome and transcriptome analysis of iron-reducing fermentative bacteria
RT Anoxybacter fermentans.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP016379; AZR73196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q9HQ97; -.
DR KEGG; aft:BBF96_07240; -.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000267250; 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: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; IPR006638; Elp3/MiaA/NifB-like_rSAM.
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; SFLDG01081; cleavage_of_the_Ca-Cb_bond_in; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 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:UP000267250};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 70..289
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 367 AA; 42663 MW; E22167DE49C6BD3D CRC64;
MSFYNEYLRY KNFNFDKFFE NITPSDILRI INEYKINEYD FLALLSPEAE NYLEDMAQKA
HRLTVQNFGK TILLYTPMYL ANYCVNRCSY CGFNIENKIK RKKLTFKEIE EEAKAISSTG
LRHILILTGE SRKETPVSYI IDAVKILRKY FDSISIEIYP LNEDEYRQVI EAGVDGLTIY
QEVYDEEIYD KVHIAGPKKN YKFRLNAPER ACRAQIRNIN IGALLGLNDW RKEAFMTGLH
AKYLQDKYSD VEVSISLPRI RPHIGVFEEI YPVNDKNLVQ IMLALRLFLP RVGITISTRE
NQNLRDNLIP LGVTKMSAGV STEVGGHTSK TKSDGQFEIS DKRSVKEIKE AILKKGYQPV
FKDWMHI
//
