ID A0A4R3YL29_9GAMM Unreviewed; 376 AA.
AC A0A4R3YL29;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=2-iminoacetate synthase {ECO:0000256|ARBA:ARBA00069280};
DE EC=4.1.99.19 {ECO:0000256|ARBA:ARBA00066802};
DE AltName: Full=Dehydroglycine synthase {ECO:0000256|ARBA:ARBA00076202};
DE AltName: Full=Tyrosine lyase {ECO:0000256|ARBA:ARBA00078269};
GN ORFNames=EDC52_11717 {ECO:0000313|EMBL:TCV91493.1};
OS Biostraticola tofi.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Bruguierivoracaceae; Biostraticola.
OX NCBI_TaxID=466109 {ECO:0000313|EMBL:TCV91493.1, ECO:0000313|Proteomes:UP000295719};
RN [1] {ECO:0000313|EMBL:TCV91493.1, ECO:0000313|Proteomes:UP000295719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19580 {ECO:0000313|EMBL:TCV91493.1,
RC ECO:0000313|Proteomes:UP000295719};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the radical-mediated cleavage of tyrosine to 2-
CC iminoacetate and 4-cresol. {ECO:0000256|ARBA:ARBA00056430}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine + S-adenosyl-L-methionine + NADPH = 2-iminoacetate
CC + 4-methylphenol + 5'-deoxyadenosine + L-methionine + NADP(+);
CC Xref=Rhea:RHEA:26361, ChEBI:CHEBI:17319, ChEBI:CHEBI:17847,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57844, ChEBI:CHEBI:58315,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:59789, ChEBI:CHEBI:77846;
CC EC=4.1.99.19; Evidence={ECO:0000256|ARBA:ARBA00052130};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
CC -!- SUBUNIT: Forms a heterodimer with ThiG.
CC {ECO:0000256|ARBA:ARBA00063197}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. ThiH family.
CC {ECO:0000256|ARBA:ARBA00061652}.
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:TCV91493.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SMCR01000017; TCV91493.1; -; Genomic_DNA.
DR RefSeq; WP_131867842.1; NZ_SMCR01000017.1.
DR AlphaFoldDB; A0A4R3YL29; -.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000295719; 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 FunFam; 3.20.20.70:FF:000122; 2-iminoacetate synthase ThiH; 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 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000295719};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 71..293
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 376 AA; 42735 MW; C8B6F5550EFCEFB6 CRC64;
MNTFTAHWQA LDWDDVGLRI HSKTSRDVAQ ALSADALAID DFMALLSPAA LPYLEPMAQQ
AQKLTRQRFG NIVGFYLPLY LSNLCANDCT YCGFSMSNPI KRKTLGEQEI INECRAIKNK
GVEHVLLVTG EHQTKVGMDY FRRYIPLIRE FFSSLMMEVQ PLSQQEYAEL KILGLDGVLV
YQETYHQATY HQHHLRGKKQ DFAWRLETPD RLARAGIDKI GLGALIGLSD NWRTDCYMVA
EHLLYLQKQY WQSRYSLSFP RLRPCAGGIT PATQMSEAQL IQVMCAFRLL APDVELSLST
RESPWFRDNA VPIMVNSISA GSKTQPGGYA NEKPELEQFL PHDNRQPSEV ADMLVRAGIQ
PVWKDWDGYL GRPAAQ
//
