P30140 (THIH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	response to DNA damage stimulus Inferred from expression pattern PubMed 11967071. Source: EcoliWiki thiamine diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	2-iminoacetate synthase activity Inferred from electronic annotation. Source: EC 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 377	377	2-iminoacetate synthase		PRO_0000072514
Sites
	Metal binding	85	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	89	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	92	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30140 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F45A0859372F5ED6	FASTA	377	43,320
	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

References

	« Hide 'large scale' referencesShow '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 277:1453-1474(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, 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.
PIR	S35121.
RefSeq	NP_418417.1. NC_000913.2. YP_491471.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P30140.
SMR	P30140. Positions 24-192.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6869N.
IntAct	P30140. 3 interactions.
STRING	511145.b3990.
Proteomic databases
PaxDb	P30140.
PRIDE	P30140.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76964; AAC76964; b3990. BAE77330; BAE77330; BAE77330.
GeneID	12933915. 948494.
KEGG	ecj:Y75_p3207. eco:b3990.
PATRIC	32123501. VBIEscCol129921_4103.
Organism-specific databases
EchoBASE	EB1548.
EcoGene	EG11590. thiH.
Phylogenomic databases
eggNOG	COG1060.
HOGENOM	HOG000270732.
KO	K03150.
OMA	NLCANEC.
ProtClustDB	PRK09240.
Enzyme and pathway databases
BioCyc	EcoCyc:THIH-MONOMER. ECOL316407:JW3953-MONOMER. MetaCyc:THIH-MONOMER.
UniPathway	UPA00060.
Gene expression databases
Genevestigator	P30140.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR010722. Biotin/thiamin_synth-assoc. IPR007197. rSAM. IPR012726. ThiH. [Graphical view]
Pfam	PF06968. BATS. 1 hit. PF04055. Radical_SAM. 1 hit. [Graphical view]
SMART	SM00876. BATS. 1 hit. [Graphical view]
TIGRFAMs	TIGR02351. thiH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

THIH_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program