P0AGG0 (THIL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thiamine-monophosphate kinase
Short name=Thiamine-phosphate kinase
EC=2.7.4.16

Gene names

Name:	thiL
Ordered Locus Names:	b0417, JW0407

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + thiamine phosphate = ADP + thiamine diphosphate.
Pathway	Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Sequence similarities	Belongs to the thiamine-monophosphate kinase family.

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	thiamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW thiamine-phosphate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 325	325	Thiamine-monophosphate kinase		PRO_0000096194
Experimental info
	Sequence conflict	254	1	A → E in BAA21778. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P0AGG0 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 9955DCE2D8CFFB8F	FASTA	325	35,071
	10 20 30 40 50 60 MACGEFSLIA RYFDRVRSSR LDVELGIGDD CALLNIPEKQ TLAISTDTLV AGNHFLPDID 70 80 90 100 110 120 PADLAYKALA VNLSDLAAMG ADPAWLTLAL TLPDVDEAWL ESFSDSLFDL LNYYDMQLIG 130 140 150 160 170 180 GDTTRGPLSM TLGIHGFVPM GRALTRSGAK PGDWIYVTGT PGDSAAGLAI LQNRLQVADA 190 200 210 220 230 240 KDADYLIKRH LRPSPRILQG QALRDLANSA IDLSDGLISD LGHIVKASDC GARIDLALLP 250 260 270 280 290 300 FSDALSRHVE PEQALRWALS GGEDYELCFT VPELNRGALD VALGHLGVPF TCIGQMTADI 310 320 EGLCFIRDGE PVTLDWKGYD HFATP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, mapping, and sequencing of the thiL gene encoding thiamine-monophosphate kinase in Escherichia coli K-12." Iida A., Hayashi M., Fujio T., Teshiba S. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases 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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D17333 Genomic DNA. Translation: BAA21778.1. U82664 Genomic DNA. Translation: AAB40173.1. U00096 Genomic DNA. Translation: AAC73520.1. AP009048 Genomic DNA. Translation: BAE76197.1.
PIR	A64771.
RefSeq	NP_414951.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0AGG0.
SMR	P0AGG0. Positions 8-310.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0AGG0. 8 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000003495; EBESCP00000003495; EBESCG00000002869. EBESCT00000018115; EBESCP00000017406; EBESCG00000017170.
GeneID	947387.
GenomeReviews	Gene locus JW0407 in contig AP009048_GR. Gene locus b0417 in contig U00096_GR.
KEGG	ecj:JW0407. eco:b0417.
PATRIC	32115983. VBIEscCol129921_0433.
Organism-specific databases
EchoBASE	EB4149.
EcoGene	EG20227. thiL.
Phylogenomic databases
eggNOG	COG0611.
GeneTree	EBGT00050000011174.
HOGENOM	HBG577902.
OMA	MGAEPAW.
PhylomeDB	P0AGG0.
ProtClustDB	PRK05731.
Enzyme and pathway databases
BioCyc	EcoCyc:THI-P-KIN-MONOMER. MetaCyc:THI-P-KIN-MONOMER.
Gene expression databases
Genevestigator	P0AGG0.
Family and domain databases
InterPro	IPR000728. AIR_synth. IPR010918. AIR_synth_C. IPR016188. PurM_N-like. IPR006283. ThiL. [Graphical view]
KO	K00946.
Pfam	PF00586. AIRS. 1 hit. PF02769. AIRS_C. 1 hit. [Graphical view]
PIRSF	PIRSF005303. Thiam_monoph_kin. 1 hit.
SUPFAM	SSF56042. AIR_synth_C. 1 hit. SSF55326. PurM_N-like. 1 hit.
TIGRFAMs	TIGR01379. ThiL. 1 hit.
ProtoNet	Search...

Entry information

Entry name

THIL_ECOLI

Accession

Primary (citable) accession number: P0AGG0
Secondary accession number(s): O32380, P77785, Q2MC09

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program