ID Q2LUU5_SYNAS Unreviewed; 371 AA.
AC Q2LUU5;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=ThiH protein {ECO:0000313|EMBL:ABC77857.1};
GN ORFNames=SYN_00439 {ECO:0000313|EMBL:ABC77857.1};
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC77857.1, ECO:0000313|Proteomes:UP000001933};
RN [1] {ECO:0000313|EMBL:ABC77857.1, ECO:0000313|Proteomes:UP000001933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB {ECO:0000313|EMBL:ABC77857.1,
RC ECO:0000313|Proteomes:UP000001933};
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP000252; ABC77857.1; -; Genomic_DNA.
DR RefSeq; WP_011417878.1; NC_007759.1.
DR AlphaFoldDB; Q2LUU5; -.
DR STRING; 56780.SYN_00439; -.
DR KEGG; sat:SYN_00439; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_046249_1_0_7; -.
DR InParanoid; Q2LUU5; -.
DR OrthoDB; 3320990at2; -.
DR Proteomes; UP000001933; 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:UP000001933};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 70..292
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 371 AA; 42209 MW; 35AA40DAF5E8D4A0 CRC64;
MSFYDVFCRY RNSEWEAVLA AVSGADIERA LQREFLDFSD FLALLSPEAE RYLEPMAQRA
RELTLRYFGR AIQLYAPIYV SDYCENACLY CSFSARNQRE RKRLSLEEVD REAKCIAETG
LRHILMLTGE SKKMSPVGYL RDCTRVLKRR FSSVAVEVYA LSEGDYAELV SEGVDGLTLY
QETYDEDLYR IIHPSGRKRD FRFRLEAPER GAAARMRQVN IGALLGLADW RQDVLFVGLH
ARYLQEQFPD VEIGASVPRL RPFVGSFQGS CRVSDKNMVQ IILALRLFIP RLGIALSTRE
DSRFRDNLIP LGITRMSAGS ATSVGGYTKA AGQNEGLPQF EIADSRTIPE IMARLREKGY
EPVLNDWIAG L
//
