ID   A0A1T5DFP0_9FIRM        Unreviewed;       482 AA.
AC   A0A1T5DFP0;
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:SKB70343.1};
GN   ORFNames=SAMN06296386_10465 {ECO:0000313|EMBL:SKB70343.1};
OS   Lachnospiraceae bacterium.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1898203 {ECO:0000313|EMBL:SKB70343.1, ECO:0000313|Proteomes:UP000191179};
RN   [1] {ECO:0000313|EMBL:SKB70343.1, ECO:0000313|Proteomes:UP000191179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH1P17 {ECO:0000313|EMBL:SKB70343.1,
RC   ECO:0000313|Proteomes:UP000191179};
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; FUZG01000004; SKB70343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5DFP0; -.
DR   OrthoDB; 9801120at2; -.
DR   Proteomes; UP000191179; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0042364; P:water-soluble vitamin biosynthetic process; IEA:UniProt.
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; IPR024007; FeFe-hyd_mat_HydG.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR034428; ThiH/NoCL/HydG-like.
DR   NCBIfam; TIGR03955; rSAM_HydG; 1.
DR   PANTHER; PTHR43583; 2-IMINOACETATE SYNTHASE; 1.
DR   PANTHER; PTHR43583:SF2; BIOTIN AND THIAMIN SYNTHESIS ASSOCIATED DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF06968; BATS; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDF00319; Fe_hydrogenase_maturase_(HydG; 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:UP000191179};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          285..392
FT                   /note="Biotin and thiamin synthesis-associated"
FT                   /evidence="ECO:0000259|SMART:SM00876"
SQ   SEQUENCE   482 AA;  54736 MW;  10FF3F3BE57E4EF7 CRC64;
     MYPYRPESMI ADEFINDDEI LQTIQFANEN KHNVELIDSL LEKARPKKKG NGVVCAGLTH
     REASVLLACD IPEKTEEMFR LANEIKQAYY GNRIVMFAPL YLSNYCINGC VYCPYHTVNK
     SIPRKKLTQE EVRNEVIALQ DMGHKRLAIE AGEDPVNNPI EYILECIKTI YSVHHKNGDI
     RRVNVNIAAT TVENYKKLKD AGIGTYILFQ ETYNKKSYLE LHPTGPKHDY NYHTEAMDRA
     MEGGIDDVGL GVLFGLEGYQ YEFAGLLMHA EHLEAVHGVG PHTISVPRVK KADDIDPGVF
     DNGLSDDKFA KIIACIRIAV PYTGMIISTR ESEAVRGRVL DYGISQISGA SRTSVGGYTE
     AERPHDTEQF DVSDNRSLDE VVRWLMENDH IPSFCTACYR EGRTGDRFMA LCKNGQILNC
     CHPNALMTLS EYLEDYASEE TKKIGYELIE QELKKIPHDN VRRIATENIE AIRSSDRRDF
     RF
//