THIH_SALTY
ID THIH_SALTY Reviewed; 377 AA.
AC Q9S498;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=2-iminoacetate synthase;
DE EC=4.1.99.19;
DE AltName: Full=Dehydroglycine synthase;
DE AltName: Full=Tyrosine lyase;
GN Name=thiH; OrderedLocusNames=STM4159; ORFNames=STMF1.38;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Webb E.A., Downs D.M.;
RT "Genetic evidence for the role of ThiH in thiazole synthesis: a model to
RT explain conditional thiazole auxotrophs.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF ASP-41; ALA-50; ALA-61; ASN-87; CYS-89;
RP TYR-91; ARG-102; GLY-130; GLU-131; GLU-187; CYS-285; GLN-338 AND TRP-363.
RC STRAIN=LT2 / DM1;
RX PubMed=15271986; DOI=10.1074/jbc.m403985200;
RA Martinez-Gomez N.C., Robers M., Downs D.M.;
RT "Mutational analysis of ThiH, a member of the radical S-adenosylmethionine
RT (AdoMet) protein superfamily.";
RL J. Biol. Chem. 279:40505-40510(2004).
CC -!- FUNCTION: Catalyzes the radical-mediated cleavage of tyrosine to 2-
CC iminoacetate and 4-cresol. {ECO:0000269|PubMed:15271986}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine + NADPH + S-adenosyl-L-methionine = 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;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- SUBUNIT: Forms a heterodimer with ThiG. {ECO:0000250}.
CC -!- MISCELLANEOUS: The product 2-iminoacetate hydrates in vitro to yield
CC glyoxylate and ammonium.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. ThiH family.
CC {ECO:0000305}.
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DR EMBL; AF154064; AAD48429.1; -; Genomic_DNA.
DR EMBL; AF170176; AAF33524.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22987.1; -; Genomic_DNA.
DR RefSeq; NP_463028.1; NC_003197.2.
DR RefSeq; WP_000847565.1; NC_003197.2.
DR AlphaFoldDB; Q9S498; -.
DR SMR; Q9S498; -.
DR STRING; 99287.STM4159; -.
DR PaxDb; Q9S498; -.
DR PRIDE; Q9S498; -.
DR DNASU; 1255685; -.
DR EnsemblBacteria; AAL22987; AAL22987; STM4159.
DR GeneID; 1255685; -.
DR KEGG; stm:STM4159; -.
DR PATRIC; fig|99287.12.peg.4373; -.
DR HOGENOM; CLU_046249_1_0_6; -.
DR OMA; LICAYRL; -.
DR PhylomeDB; Q9S498; -.
DR BioCyc; SENT99287:STM4159-MON; -.
DR BRENDA; 4.1.99.19; 5542.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000001014; Chromosome.
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 GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR43583; PTHR43583; 1.
DR PANTHER; PTHR43583:SF1; PTHR43583:SF1; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00301; 2-iminoacetate_synthase_(ThiH); 1.
DR SMART; SM00876; BATS; 1.
DR TIGRFAMs; TIGR02351; thiH; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; NADP; Reference proteome;
KW S-adenosyl-L-methionine; Thiamine biosynthesis.
FT CHAIN 1..377
FT /note="2-iminoacetate synthase"
FT /id="PRO_0000072515"
FT DOMAIN 71..301
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT MUTAGEN 41
FT /note="D->V: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
FT MUTAGEN 50
FT /note="A->T: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
FT MUTAGEN 61
FT /note="A->T: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
FT MUTAGEN 87
FT /note="N->A,K: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
FT MUTAGEN 89
FT /note="C->A: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
FT MUTAGEN 91
FT /note="Y->A: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
FT MUTAGEN 102
FT /note="R->P: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
FT MUTAGEN 130
FT /note="G->A: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
FT MUTAGEN 131
FT /note="E->A,K: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
FT MUTAGEN 187
FT /note="E->D: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
FT MUTAGEN 285
FT /note="C->H: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
FT MUTAGEN 338
FT /note="Q->L: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
FT MUTAGEN 363
FT /note="W->C: No activity."
FT /evidence="ECO:0000269|PubMed:15271986"
SQ SEQUENCE 377 AA; 43447 MW; 814A5840C948879A CRC64;
MKTFTDRWRQ LEWDDIRLRI NGKTAADVER ALNAAHLSRD DLMALLSPAA ADYLEPIAQR
AQRLTRQRFG NTVSFYVPLY LSNLCANDCT YCGFSMSNRI KRKTLDEVDI QRECDAIRKL
GFEHLLLVTG EHQAKVGMDY FRRHLPTIRR QFSSLQMEVQ PLSQENYAEL KTLGIDGVMV
YQETYHEAIY AQHHLKGKKQ DFFWRLETPD RLGRAGIDKI GLGALIGLSD NWRVDCYMVA
EHLLWMQKHY WQSRYSVSFP RLRPCTGGVE PASVMDEKQL VQTICAFRLL APEIELSLST
RESPWFRDHV IPLAINNVSA FSKTQPGGYA DDHPELEQFS PHDARRPETV ASALSAQGLQ
PVWKDWDSWL GRASQTR
