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Database: UniProt
Entry: A0A396QCW7_9FIRM
LinkDB: A0A396QCW7_9FIRM
Original site: A0A396QCW7_9FIRM 
ID   A0A396QCW7_9FIRM        Unreviewed;       404 AA.
AC   A0A396QCW7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=2-iminoacetate synthase ThiH {ECO:0000313|EMBL:RHV86854.1};
GN   ORFNames=DXA96_14715 {ECO:0000313|EMBL:RHV86854.1};
OS   Lachnospiraceae bacterium OF09-33XD.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=2292273 {ECO:0000313|EMBL:RHV86854.1, ECO:0000313|Proteomes:UP000265865};
RN   [1] {ECO:0000313|EMBL:RHV86854.1, ECO:0000313|Proteomes:UP000265865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OF09-33XD {ECO:0000313|EMBL:RHV86854.1,
RC   ECO:0000313|Proteomes:UP000265865};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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:RHV86854.1}.
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DR   EMBL; QUME01000031; RHV86854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A396QCW7; -.
DR   Proteomes; UP000265865; 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:UP000265865};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          290..396
FT                   /note="Biotin and thiamin synthesis-associated"
FT                   /evidence="ECO:0000259|SMART:SM00876"
SQ   SEQUENCE   404 AA;  46406 MW;  8C094D7352F67737 CRC64;
     MSTDQINDSI FSDEIKEHLK ENRIDHMTYL PGMEDVGTDI QEQVISRMKD YDYDQYTEAD
     VRRALSHERR TPEDFAALLS PAALSCLEEM AQRAREETRK HFGNSVYMFT PLYIANYCEN
     YCIYCGFNCH NKIRRARLTP DEIRREMEAI SKTGLQEILI LTGESRAKSD VEYIGQACRI
     AKDYFRVIGL EVYPMNSDEY AYLHQCGADY VTVFQETYDS DKYETLHLAG HKRIFPYRLN
     AQERALQGGM RGVGFAALLG LTDFRKDAYA TGIHAWLIQR KYPHAEIAFS CPRLRPIINN
     EKINPMDVHE RQLLQVVSAY RLFMPFASIT VSTRECARVR DNLVQIAATK ISAGVSTGIG
     SHVEELEDKG DEQFEISDGR SVEEVFQALV QQDLQPVMAD YVYV
//
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