O31620 (THID_BACSU) 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:	yjbV
Ordered Locus Names:	BSU11710

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	271 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. Ref.2
Catalytic activity	ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine. Ref.2 ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine. Ref.2
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.
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 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 – 271	271	Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase		PRO_0000391753
Sites
	Binding site	44	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O31620 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 1554AD7F253F983D	FASTA	271	29,124
	10 20 30 40 50 60 MSIYKALTIA GSDSGGGAGI QADIKTFQEL DVFGMSAITA VTAQNTLGVH GVHPLTVETL 70 80 90 100 110 120 RQQIDAVAED LRPDAVKTGM LWNADMIEEV ARKIDEYGFN RVIVDPVMIA KGGASLLRDE 130 140 150 160 170 180 SVATLKELLI PRSYAITPNV PEAETLTGMT ISSLDDRKKA AEQLVKMGAQ HVIIKGGHQP 190 200 210 220 230 240 EDNHITDLLF DGSMFMQITH PYINTKHTHG TGCTFAAALT AQTAKGDSIH QAFEVAANFV 250 260 270 REAVENTLGI GSGHGPTNHF AFKRNSLNTS R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[2]	"Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase and pyridoxal kinase." Park J.-H., Burns K., Kinsland C., Begley T.P. J. Bacteriol. 186:1571-1573(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS HMP AND HMP-P KINASE, CATALYTIC ACTIVITY. Strain: 168 / CU1065.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL009126 Genomic DNA. Translation: CAB13028.1.
PIR	F69845.
RefSeq	NP_389053.1. NC_000964.3.
3D structure databases
HSSP	HSSP built from PDB template 1JXH based on UniProtKB P55882.
ProteinModelPortal	O31620.
SMR	O31620. Positions 3-261.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU11710.
Proteomic databases
PaxDb	O31620.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB13028; CAB13028; BSU11710.
GeneID	936415.
KEGG	bsu:BSU11710.
PATRIC	18974059. VBIBacSub10457_1223.
Organism-specific databases
GenoList	BSU11710. [Micado]
Phylogenomic databases
eggNOG	COG0351.
HOGENOM	HOG000225273.
KO	K00941.
OMA	ETCDFGL.
ProtClustDB	PRK06427.
Enzyme and pathway databases
BioCyc	BSUB:BSU11710-MONOMER. MetaCyc:BSU11710-MONOMER.
UniPathway	UPA00060; UER00137. UPA00060; UER00138.
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_BACSU

Accession

Primary (citable) accession number: O31620

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 2, 2010
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program