ID D3PAV9_DEFDS Unreviewed; 372 AA.
AC D3PAV9;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Thiamine biosynthesis protein ThiH {ECO:0000313|EMBL:BAI79732.1};
GN Name=thiH {ECO:0000313|EMBL:BAI79732.1};
GN OrderedLocusNames=DEFDS_0221 {ECO:0000313|EMBL:BAI79732.1};
OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS SSM1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Deferribacteraceae; Deferribacter.
OX NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI79732.1, ECO:0000313|Proteomes:UP000001520};
RN [1] {ECO:0000313|EMBL:BAI79732.1, ECO:0000313|Proteomes:UP000001520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC {ECO:0000313|Proteomes:UP000001520};
RX PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA Takai K.;
RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT the genome sequence of the thermophilic bacterium Deferribacter
RT desulfuricans SSM1.";
RL DNA Res. 17:123-137(2010).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; AP011529; BAI79732.1; -; Genomic_DNA.
DR RefSeq; WP_013006980.1; NC_013939.1.
DR AlphaFoldDB; D3PAV9; -.
DR STRING; 639282.DEFDS_0221; -.
DR KEGG; ddf:DEFDS_0221; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_046249_1_0_0; -.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000001520; 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; 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; SFLDG01060; BATS_domain_containing; 1.
DR SMART; SM00876; BATS; 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:UP000001520};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 70..299
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 372 AA; 42702 MW; 2CAC99E426F2C863 CRC64;
MSFYDIYKEY NWEEIKDFIY SRRENDVIDI LFKENLSVED FATLLSPAAE KFLEDMAQKA
HKITVMRFGK TIKLYAPLYL SNVCQNACTY CGFNVFHKIP RITLKKDEIE REAKAVADTG
IKHILLLTGE APNVATLEYL KEAVSICNKY FSSIGIEIYP LDINGYKELI DVGVDYLTIY
QETYNRETYD KIHPKGKKKD LLWRLETPER GAIAGMRTVG IGALMGLEDF RVDEFFVGLH
AKYLMKKYWK THITVSFPRM RKAPGVDTPF VEVSDKNLVQ SMLAMRIFLH DVGIVISTRE
PANLRDNLIP LGVTQMSAGS KTEPGGYSLK EDENAEQFHI EDNRSVDEII NVIRSKGYDP
VLKDWDRAFV IA
//
