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P30140 (THIH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-iminoacetate synthase

EC=4.1.99.19
Alternative name(s):
Dehydroglycine synthase
Tyrosine lyase
Gene names
Name:thiH
Ordered Locus Names:b3990, JW3953
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the radical-mediated cleavage of tyrosine to 2-iminoacetate and 4-cresol. Ref.7 Ref.8

Catalytic activity

L-tyrosine + S-adenosyl-L-methionine + reduced acceptor = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + acceptor + 2 H+. Ref.7 Ref.8

Cofactor

Binds 1 4Fe-4S cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Ref.6 Ref.8

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis.

Subunit structure

Forms a heterodimer with ThiG. Ref.6

Miscellaneous

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

Sequence similarities

Belongs to the radical SAM superfamily. ThiH family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

thiGP301392EBI-1125553,EBI-547059

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3773772-iminoacetate synthase
PRO_0000072514

Sites

Metal binding851Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding891Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding921Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
P30140 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F45A0859372F5ED6

FASTA37743,320
        10         20         30         40         50         60 
MKTFSDRWRQ LDWDDIRLRI NGKTAADVER ALNASQLTRD DMMALLSPAA SGYLEQLAQR 

        70         80         90        100        110        120 
AQRLTRQRFG NTVSFYVPLY LSNLCANDCT YCGFSMSNRI KRKTLDEADI ARESAAIREM 

       130        140        150        160        170        180 
GFEHLLLVTG EHQAKVGMDY FRRHLPALRE QFSSLQMEVQ PLAETEYAEL KQLGLDGVMV 

       190        200        210        220        230        240 
YQETYHEATY ARHHLKGKKQ DFFWRLETPD RLGRAGIDKI GLGALIGLSD NWRVDSYMVA 

       250        260        270        280        290        300 
EHLLWLQQHY WQSRYSVSFP RLRPCTGGIE PASIMDERQL VQTICAFRLL APEIELSLST 

       310        320        330        340        350        360 
RESPWFRDRV IPLAINNVSA FSKTQPGGYA DNHPELEQFS PHDDRRPEAV AAALTAQGLQ 

       370 
PVWKDWDSYL GRASQRL 

« Hide

References

« Hide 'large scale' references
[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(1993) [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(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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(2006) [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(1998) [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(2003) [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(2007) [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(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, EPR SPECTROSCOPY, COFACTOR, CATALYTIC ACTIVITY, REACTION MECHANISM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M88701 Genomic DNA. Translation: AAB95619.1.
U00006 Genomic DNA. Translation: AAC43088.1.
U00096 Genomic DNA. Translation: AAC76964.1.
AP009048 Genomic DNA. Translation: BAE77330.1.
PIRS35121.
RefSeqNP_418417.1. NC_000913.3.
YP_491471.1. NC_007779.1.

3D structure databases

ProteinModelPortalP30140.
SMRP30140. Positions 24-228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6869N.
IntActP30140. 4 interactions.
STRING511145.b3990.

Proteomic databases

PaxDbP30140.
PRIDEP30140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76964; AAC76964; b3990.
BAE77330; BAE77330; BAE77330.
GeneID12933915.
948494.
KEGGecj:Y75_p3207.
eco:b3990.
PATRIC32123501. VBIEscCol129921_4103.

Organism-specific databases

EchoBASEEB1548.
EcoGeneEG11590. thiH.

Phylogenomic databases

eggNOGCOG1060.
HOGENOMHOG000270732.
KOK03150.
OMAQLICAYR.
OrthoDBEOG6RNQB0.
PhylomeDBP30140.
ProtClustDBPRK09240.

Enzyme and pathway databases

BioCycEcoCyc:THIH-MONOMER.
ECOL316407:JW3953-MONOMER.
MetaCyc:THIH-MONOMER.
UniPathwayUPA00060.

Gene expression databases

GenevestigatorP30140.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR007197. rSAM.
IPR012726. ThiH.
[Graphical view]
PfamPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTSM00876. BATS. 1 hit.
[Graphical view]
TIGRFAMsTIGR02351. thiH. 1 hit.
ProtoNetSearch...

Other

PROP30140.

Entry information

Entry nameTHIH_ECOLI
AccessionPrimary (citable) accession number: P30140
Secondary accession number(s): Q2M8S6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene