ID A0A1T4LGL1_9FIRM Unreviewed; 417 AA.
AC A0A1T4LGL1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=2-iminoacetate synthase {ECO:0000313|EMBL:SJZ53823.1};
GN ORFNames=SAMN02745110_00846 {ECO:0000313|EMBL:SJZ53823.1};
OS Eubacterium ruminantium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=42322 {ECO:0000313|EMBL:SJZ53823.1, ECO:0000313|Proteomes:UP000189857};
RN [1] {ECO:0000313|EMBL:SJZ53823.1, ECO:0000313|Proteomes:UP000189857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17233 {ECO:0000313|EMBL:SJZ53823.1,
RC ECO:0000313|Proteomes:UP000189857};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUXA01000005; SJZ53823.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4LGL1; -.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000189857; 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 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.
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:UP000189857};
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; 47849 MW; 6F4C88FA796F6A7A CRC64;
MENNYLIDSD NLSPEALERK HRLENDPSLR TNHMEYLPGM QKIESDVCKN VLEQMNSYDH
SKYTAKDVMR ALEHETCSIE DFKALLSPAA EPFLEKMAQR AKIETSKHFG NTVYLFTPIY
IANYCENYCV YCGFNCYNKI RRMKLTMEQI EHEMKVIADS GMEEVLLLTG ESRAMSDVEY
IGEACKLARK YFRLVGLEIY PVNVDEYKYL HECGADYVTV FQETYDTVKY ETLHLMGNKR
VWPYRFDAQE RALMGGMRGV AFSALLGLSD FRKDAFATAL HVYYLQRKYP HAEMSLSCPR
LRPIVNNDKI SPLDVHEKQL CQIICAYRIF LPFVGITVSS RESAEFRNGI VKIAATKVSA
GVSTGIGDHE SKYSGKDSTG EEGDEQFEIC DSRSLDAMYN DITDEGLQPV MNDYLYV
//
