ID F7JMA8_9FIRM Unreviewed; 417 AA.
AC F7JMA8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Thiazole biosynthesis protein ThiH {ECO:0000313|EMBL:EGN38274.1};
GN ORFNames=HMPREF0988_01513 {ECO:0000313|EMBL:EGN38274.1};
OS Lachnospiraceae bacterium 1_4_56FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658655 {ECO:0000313|EMBL:EGN38274.1, ECO:0000313|Proteomes:UP000004289};
RN [1] {ECO:0000313|EMBL:EGN38274.1, ECO:0000313|Proteomes:UP000004289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_4_56FAA {ECO:0000313|EMBL:EGN38274.1,
RC ECO:0000313|Proteomes:UP000004289};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 1_4_56FAA.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGN38274.1}.
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DR EMBL; ACTN01000010; EGN38274.1; -; Genomic_DNA.
DR AlphaFoldDB; F7JMA8; -.
DR STRING; 658655.HMPREF0988_01513; -.
DR PATRIC; fig|658655.3.peg.1535; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_046249_1_0_9; -.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000004289; 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:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
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; SFLDS00029; Radical_SAM; 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:UP000004289};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 297..409
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
SQ SEQUENCE 417 AA; 47791 MW; A920EC57216A6169 CRC64;
MDNQFFVDSE HLSPEALAKK HRLENNPSSR KSHMEYLPGM EVIESDVCAS VMAQMNSYDY
SKYTAADVKA ALEHDTCMIE DFKALLSPAA EPFLEQMAQR ARLETSKHFG NTVYLFTPLY
IANYCENYCV YCGFNCYNHI NRMKLSMEQI EKEMKVIADS GMEEILILTG ESRGQSNVEY
IGEACKLARK YFRMVGLEIY PVNTDEYKYL HECGADYVTV FQETYDADRY EQLHLLGHKR
VWPYRFDAQE RALRGGMRGV AFSALLGLSD FRKDALASAL HVYYLQRKYP HAEMSLSCPR
LRPIINNDKI NPLDVHEKQL CQVLCAYRIF LPYVGITVSS RESAEFRNGI VKIAATKVSA
GVSTGIGDHE SKYTGKETDE VQGDEQFEID DNRSLDKMYR DIAEEGLQPV LNDYLYV
//
