P76422 (THID_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
EC=2.7.1.49
EC=2.7.4.7

Alternative name(s):
Hydroxymethylpyrimidine kinase
Short name=HMP kinase
Hydroxymethylpyrimidine phosphate kinase
Short name=HMP-P kinase
Short name=HMP-phosphate kinase
Short name=HMPP kinase

Gene names

Name:	thiD
Synonyms:	thiJ
Ordered Locus Names:	b2103, JW2090

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	266 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity with pyridoxal, pyridoxamine or pyridoxine.
Catalytic activity	ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine. Ref.1 ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine. Ref.1
Pathway	Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 2/3. Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.
Subunit structure	Monomer. Ref.1
Sequence similarities	Belongs to the ThiD family.

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	thiamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW thiamine diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydroxymethylpyrimidine kinase activity Inferred from electronic annotation. Source: EC phosphomethylpyrimidine 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 – 266	266	Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase		PRO_0000192018
Sites
	Binding site	44	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P76422 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: E555CEFE445B8F0A	FASTA	266	28,634
	10 20 30 40 50 60 MKRINALTIA GTDPSGGAGI QADLKTFSAL GAYGCSVITA LVAQNTRGVQ SVYRIEPDFV 70 80 90 100 110 120 AAQLDSVFSD VRIDTTKIGM LAETDIVEAV AERLQRYQIQ NVVLDTVMLA KSGDPLLSPS 130 140 150 160 170 180 AVATLRSRLL PQVSLITPNL PEAAALLDAP HARTEQEMLE QGRSLLAMGC GAVLMKGGHL 190 200 210 220 230 240 DDEQSPDWLF TREGEQRFTA PRIMTKNTHG TGCTLSAALA ALRPRHTNWA DTVQEAKSWL 250 260 SSALAQADTL EVGHGIGPVH HFHAWW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of the thiD/J gene of Escherichia coli encoding a thiamin-synthesizing bifunctional enzyme, hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase." Mizote T., Tsuda M., Smith D.D.S., Nakayama H., Nakazawa T. Microbiology 145:495-501(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, CATALYTIC ACTIVITY, SUBUNIT. Strain: K12.
[2]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D84200 Genomic DNA. Translation: BAA76742.1. U00096 Genomic DNA. Translation: AAC75164.1. AP009048 Genomic DNA. Translation: BAA15971.1.
PIR	F64977.
RefSeq	NP_416606.1. NC_000913.2. YP_490343.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P76422.
SMR	P76422. Positions 1-266.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6867N.
IntAct	P76422. 7 interactions.
STRING	511145.b2103.
Proteomic databases
PaxDb	P76422.
PRIDE	P76422.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75164; AAC75164; b2103. BAA15971; BAA15971; BAA15971.
GeneID	12932542. 946459.
KEGG	ecj:Y75_p2065. eco:b2103.
PATRIC	32119539. VBIEscCol129921_2180.
Organism-specific databases
EchoBASE	EB3821.
EcoGene	EG14068. thiD.
Phylogenomic databases
eggNOG	COG0351.
HOGENOM	HOG000225275.
KO	K00941.
OMA	ETCDFGL.
ProtClustDB	PRK06427.
Enzyme and pathway databases
BioCyc	EcoCyc:HMP-P-KIN-MONOMER. ECOL316407:JW2090-MONOMER. MetaCyc:HMP-P-KIN-MONOMER.
UniPathway	UPA00060; UER00137. UPA00060; UER00138.
Gene expression databases
Genevestigator	P76422.
Family and domain databases
InterPro	IPR013749. HMP-P_kinase-1. IPR004399. HMP-P_kinase-2. [Graphical view]
Pfam	PF08543. Phos_pyr_kin. 1 hit. [Graphical view]
TIGRFAMs	TIGR00097. HMP-P_kinase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

THID_ECOLI

Accession

Primary (citable) accession number: P76422

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program