THIH_ECOLI
ID THIH_ECOLI Reviewed; 377 AA.
AC P30140; Q2M8S6;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=2-iminoacetate synthase;
DE EC=4.1.99.19 {ECO:0000269|PubMed:17403671, ECO:0000269|PubMed:17969213};
DE AltName: Full=Dehydroglycine synthase;
DE AltName: Full=Tyrosine lyase;
GN Name=thiH; OrderedLocusNames=b3990, JW3953;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8432721; DOI=10.1128/jb.175.4.982-992.1993;
RA Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P.;
RT "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in
RT Escherichia coli K-12.";
RL J. Bacteriol. 175:982-992(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 41-47, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10082377; DOI=10.1002/pro.5560070815;
RA Kelleher N.L., Taylor S.V., Grannis D., Kinsland C., Chiu H.-J.,
RA Begley T.P., McLafferty F.W.;
RT "Efficient sequence analysis of the six gene products (7-74 kDa) from the
RT Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass
RT spectrometry.";
RL Protein Sci. 7:1796-1801(1998).
RN [6]
RP INTERACTION WITH THIG, SUBUNIT, EPR SPECTROSCOPY, AND COFACTOR.
RX PubMed=12650933; DOI=10.1016/s0014-5793(03)00204-7;
RA Leonardi R., Fairhurst S.A., Kriek M., Lowe D.J., Roach P.L.;
RT "Thiamine biosynthesis in Escherichia coli: isolation and initial
RT characterisation of the ThiGH complex.";
RL FEBS Lett. 539:95-99(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, REACTION PRODUCTS, AND REACTION MECHANISM.
RX PubMed=17969213; DOI=10.1002/anie.200702554;
RA Kriek M., Martins F., Challand M.R., Croft A., Roach P.L.;
RT "Thiamine biosynthesis in Escherichia coli: identification of the
RT intermediate and by-product derived from tyrosine.";
RL Angew. Chem. Int. Ed. 46:9223-9226(2007).
RN [8]
RP FUNCTION, EPR SPECTROSCOPY, COFACTOR, CATALYTIC ACTIVITY, AND REACTION
RP MECHANISM.
RX PubMed=17403671; DOI=10.1074/jbc.m700782200;
RA Kriek M., Martins F., Leonardi R., Fairhurst S.A., Lowe D.J., Roach P.L.;
RT "Thiazole synthase from Escherichia coli: an investigation of the
RT substrates and purified proteins required for activity in vitro.";
RL J. Biol. Chem. 282:17413-17423(2007).
CC -!- FUNCTION: Catalyzes the radical-mediated cleavage of tyrosine to 2-
CC iminoacetate and 4-cresol. {ECO:0000269|PubMed:17403671,
CC ECO:0000269|PubMed:17969213}.
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; Evidence={ECO:0000269|PubMed:17403671,
CC ECO:0000269|PubMed:17969213};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:12650933, ECO:0000269|PubMed:17403671};
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:0000269|PubMed:12650933, ECO:0000269|PubMed:17403671};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- SUBUNIT: Forms a heterodimer with ThiG. {ECO:0000269|PubMed:12650933}.
CC -!- INTERACTION:
CC P30140; P30139: thiG; NbExp=2; IntAct=EBI-1125553, EBI-547059;
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; M88701; AAB95619.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43088.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76964.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77330.1; -; Genomic_DNA.
DR PIR; S35121; S35121.
DR RefSeq; NP_418417.1; NC_000913.3.
DR RefSeq; WP_000847447.1; NZ_SSZK01000047.1.
DR AlphaFoldDB; P30140; -.
DR SMR; P30140; -.
DR BioGRID; 4262909; 13.
DR ComplexPortal; CPX-2135; thiG-thiH thiazole phosphate synthase complex.
DR DIP; DIP-6869N; -.
DR IntAct; P30140; 4.
DR STRING; 511145.b3990; -.
DR PaxDb; P30140; -.
DR PRIDE; P30140; -.
DR EnsemblBacteria; AAC76964; AAC76964; b3990.
DR EnsemblBacteria; BAE77330; BAE77330; BAE77330.
DR GeneID; 948494; -.
DR KEGG; ecj:JW3953; -.
DR KEGG; eco:b3990; -.
DR PATRIC; fig|1411691.4.peg.2722; -.
DR EchoBASE; EB1548; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_046249_1_0_6; -.
DR InParanoid; P30140; -.
DR OMA; LICAYRL; -.
DR PhylomeDB; P30140; -.
DR BioCyc; EcoCyc:THIH-MON; -.
DR BioCyc; MetaCyc:THIH-MON; -.
DR BRENDA; 4.1.99.19; 2026.
DR UniPathway; UPA00060; -.
DR PRO; PR:P30140; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1902508; C:2-iminoacetate synthase complex; IPI:ComplexPortal.
DR GO; GO:0036355; F:2-iminoacetate synthase activity; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:EcoCyc.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IDA:ComplexPortal.
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 SFLD; SFLDS00029; Radical_SAM; 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; Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding;
KW NADP; Reference proteome; S-adenosyl-L-methionine; Thiamine biosynthesis.
FT CHAIN 1..377
FT /note="2-iminoacetate synthase"
FT /id="PRO_0000072514"
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"
SQ SEQUENCE 377 AA; 43320 MW; F45A0859372F5ED6 CRC64;
MKTFSDRWRQ LDWDDIRLRI NGKTAADVER ALNASQLTRD DMMALLSPAA SGYLEQLAQR
AQRLTRQRFG NTVSFYVPLY LSNLCANDCT YCGFSMSNRI KRKTLDEADI ARESAAIREM
GFEHLLLVTG EHQAKVGMDY FRRHLPALRE QFSSLQMEVQ PLAETEYAEL KQLGLDGVMV
YQETYHEATY ARHHLKGKKQ DFFWRLETPD RLGRAGIDKI GLGALIGLSD NWRVDSYMVA
EHLLWLQQHY WQSRYSVSFP RLRPCTGGIE PASIMDERQL VQTICAFRLL APEIELSLST
RESPWFRDRV IPLAINNVSA FSKTQPGGYA DNHPELEQFS PHDDRRPEAV AAALTAQGLQ
PVWKDWDSYL GRASQRL
