ID A0A377GWK9_9FUSO Unreviewed; 385 AA.
AC A0A377GWK9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE SubName: Full=2-iminoacetate synthase {ECO:0000313|EMBL:STO31316.1};
DE EC=4.1.99.19 {ECO:0000313|EMBL:STO31316.1};
GN Name=thiH_1 {ECO:0000313|EMBL:STO31316.1};
GN ORFNames=NCTC10723_00764 {ECO:0000313|EMBL:STO31316.1};
OS Fusobacterium necrogenes.
OC Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia; Fusobacteriales;
OC Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=858 {ECO:0000313|EMBL:STO31316.1, ECO:0000313|Proteomes:UP000255328};
RN [1] {ECO:0000313|EMBL:STO31316.1, ECO:0000313|Proteomes:UP000255328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10723 {ECO:0000313|EMBL:STO31316.1,
RC ECO:0000313|Proteomes:UP000255328};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; UGGU01000003; STO31316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A377GWK9; -.
DR Proteomes; UP000255328; Unassembled WGS sequence.
DR GO; GO:0036355; F:2-iminoacetate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; 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; IPR058240; rSAM_sf.
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 SFLD; SFLDG01081; cleavage_of_the_Ca-Cb_bond_in; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00876; BATS; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:STO31316.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000255328};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 87..316
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 385 AA; 44160 MW; 47C0E15275BEE90F CRC64;
MLVLHHHLQD FCLEVSRMSY YDELVKWKGF DFEGYFNSVT DGEILKSIEK DKLSVYDYLN
LLSPRAKNHI EKMAQRAHKL TRQYFGNVIG LYLPIYVSNY CTSNCIYCGF SKKNHIVRRH
MKFEEIEREA KEIAKSGIEN ILLLTGEAKG LVDKEYLKGG IDVLKKYFSS VSIEVMPLDE
EDYRYLAKDG LDGLTVYQET YDEKRYAEVH LSGEKRDFKY RLDTPERGAK AGLRTIGIGA
LLGLGNIRSD AFKTGLHLKY LIDNYPNSEF SISFPRVNEA EGNLKDSYAV DDITFVQIIL
ANRIFQPTAG ITLSTRESAY MRDNLLQLGI TKFSAGSKTE VGGYSHENES TAQFDITDNR
SVEEIVEAIR KRGLEPKYKD WETLL
//
