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Protein

2-iminoacetate synthase

Gene

thiH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the radical-mediated cleavage of tyrosine to 2-iminoacetate and 4-cresol.2 Publications

Catalytic activityi

L-tyrosine + S-adenosyl-L-methionine + NADPH = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + NADP+ + H+.2 Publications

Cofactori

[4Fe-4S] cluster2 PublicationsNote: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi85 – 851Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi89 – 891Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi92 – 921Iron-sulfur (4Fe-4S-S-AdoMet)By similarity

GO - Molecular functioni

  1. 2-iminoacetate synthase activity Source: UniProtKB-EC
  2. 4 iron, 4 sulfur cluster binding Source: EcoCyc
  3. iron ion binding Source: InterPro
  4. iron-sulfur cluster binding Source: EcoCyc
  5. lyase activity Source: EcoCyc

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: EcoliWiki
  2. thiamine biosynthetic process Source: EcoCyc
  3. thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciEcoCyc:THIH-MONOMER.
ECOL316407:JW3953-MONOMER.
MetaCyc:THIH-MONOMER.
BRENDAi4.1.99.19. 2026.
UniPathwayiUPA00060.

Names & Taxonomyi

Protein namesi
Recommended name:
2-iminoacetate synthase (EC:4.1.99.192 Publications)
Alternative name(s):
Dehydroglycine synthase
Tyrosine lyase
Gene namesi
Name:thiH
Ordered Locus Names:b3990, JW3953
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11590. thiH.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3773772-iminoacetate synthasePRO_0000072514Add
BLAST

Proteomic databases

PaxDbiP30140.
PRIDEiP30140.

Expressioni

Gene expression databases

GenevestigatoriP30140.

Interactioni

Subunit structurei

Forms a heterodimer with ThiG.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
thiGP301392EBI-1125553,EBI-547059

Protein-protein interaction databases

DIPiDIP-6869N.
IntActiP30140. 4 interactions.
STRINGi511145.b3990.

Structurei

3D structure databases

ProteinModelPortaliP30140.
SMRiP30140. Positions 13-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. ThiH family.Curated

Phylogenomic databases

eggNOGiCOG1060.
HOGENOMiHOG000270732.
InParanoidiP30140.
KOiK03150.
OMAiLEQFEIS.
OrthoDBiEOG6RNQB0.
PhylomeDBiP30140.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR007197. rSAM.
IPR012726. ThiH.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00876. BATS. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02351. thiH. 1 hit.

Sequencei

Sequence statusi: Complete.

P30140-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTFSDRWRQ LDWDDIRLRI NGKTAADVER ALNASQLTRD DMMALLSPAA
60 70 80 90 100
SGYLEQLAQR AQRLTRQRFG NTVSFYVPLY LSNLCANDCT YCGFSMSNRI
110 120 130 140 150
KRKTLDEADI ARESAAIREM GFEHLLLVTG EHQAKVGMDY FRRHLPALRE
160 170 180 190 200
QFSSLQMEVQ PLAETEYAEL KQLGLDGVMV YQETYHEATY ARHHLKGKKQ
210 220 230 240 250
DFFWRLETPD RLGRAGIDKI GLGALIGLSD NWRVDSYMVA EHLLWLQQHY
260 270 280 290 300
WQSRYSVSFP RLRPCTGGIE PASIMDERQL VQTICAFRLL APEIELSLST
310 320 330 340 350
RESPWFRDRV IPLAINNVSA FSKTQPGGYA DNHPELEQFS PHDDRRPEAV
360 370
AAALTAQGLQ PVWKDWDSYL GRASQRL
Length:377
Mass (Da):43,320
Last modified:January 22, 2007 - v3
Checksum:iF45A0859372F5ED6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88701 Genomic DNA. Translation: AAB95619.1.
U00006 Genomic DNA. Translation: AAC43088.1.
U00096 Genomic DNA. Translation: AAC76964.1.
AP009048 Genomic DNA. Translation: BAE77330.1.
PIRiS35121.
RefSeqiNP_418417.1. NC_000913.3.
YP_491471.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76964; AAC76964; b3990.
BAE77330; BAE77330; BAE77330.
GeneIDi12933915.
948494.
KEGGiecj:Y75_p3207.
eco:b3990.
PATRICi32123501. VBIEscCol129921_4103.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88701 Genomic DNA. Translation: AAB95619.1.
U00006 Genomic DNA. Translation: AAC43088.1.
U00096 Genomic DNA. Translation: AAC76964.1.
AP009048 Genomic DNA. Translation: BAE77330.1.
PIRiS35121.
RefSeqiNP_418417.1. NC_000913.3.
YP_491471.1. NC_007779.1.

3D structure databases

ProteinModelPortaliP30140.
SMRiP30140. Positions 13-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6869N.
IntActiP30140. 4 interactions.
STRINGi511145.b3990.

Proteomic databases

PaxDbiP30140.
PRIDEiP30140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76964; AAC76964; b3990.
BAE77330; BAE77330; BAE77330.
GeneIDi12933915.
948494.
KEGGiecj:Y75_p3207.
eco:b3990.
PATRICi32123501. VBIEscCol129921_4103.

Organism-specific databases

EchoBASEiEB1548.
EcoGeneiEG11590. thiH.

Phylogenomic databases

eggNOGiCOG1060.
HOGENOMiHOG000270732.
InParanoidiP30140.
KOiK03150.
OMAiLEQFEIS.
OrthoDBiEOG6RNQB0.
PhylomeDBiP30140.

Enzyme and pathway databases

UniPathwayiUPA00060.
BioCyciEcoCyc:THIH-MONOMER.
ECOL316407:JW3953-MONOMER.
MetaCyc:THIH-MONOMER.
BRENDAi4.1.99.19. 2026.

Miscellaneous databases

PROiP30140.

Gene expression databases

GenevestigatoriP30140.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR007197. rSAM.
IPR012726. ThiH.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00876. BATS. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02351. thiH. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in Escherichia coli K-12."
    Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P.
    J. Bacteriol. 175:982-992(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Efficient sequence analysis of the six gene products (7-74 kDa) from the Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass spectrometry."
    Kelleher N.L., Taylor S.V., Grannis D., Kinsland C., Chiu H.-J., Begley T.P., McLafferty F.W.
    Protein Sci. 7:1796-1801(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 41-47, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex."
    Leonardi R., Fairhurst S.A., Kriek M., Lowe D.J., Roach P.L.
    FEBS Lett. 539:95-99(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THIG, SUBUNIT, EPR SPECTROSCOPY, COFACTOR.
  7. "Thiamine biosynthesis in Escherichia coli: identification of the intermediate and by-product derived from tyrosine."
    Kriek M., Martins F., Challand M.R., Croft A., Roach P.L.
    Angew. Chem. Int. Ed. 46:9223-9226(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION PRODUCTS, REACTION MECHANISM.
  8. "Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro."
    Kriek M., Martins F., Leonardi R., Fairhurst S.A., Lowe D.J., Roach P.L.
    J. Biol. Chem. 282:17413-17423(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, EPR SPECTROSCOPY, COFACTOR, CATALYTIC ACTIVITY, REACTION MECHANISM.

Entry informationi

Entry nameiTHIH_ECOLI
AccessioniPrimary (citable) accession number: P30140
Secondary accession number(s): Q2M8S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1993
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The product 2-iminoacetate hydrates in vitro to yield glyoxylate and ammonium.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.