Reviewed, UniProtKB/Swiss-Prot Q7WNY5 (ISPE_BORBR)

Names and origin

Protein names

Recommended name:
    4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
      Short name=CMK
    EC=2.7.1.148
Alternative name(s):
    4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase

Gene names

Name:	ispE
Synonyms:	ipk
Ordered Locus Names:	BB0900

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol By similarity. HAMAP MF_00061
Catalytic activity	ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. HAMAP MF_00061
Pathway	Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. HAMAP MF_00061
Sequence similarities	Belongs to the GHMP kinase family. IspE subfamily.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phosphorylation Inferred from electronic annotation. Source: InterPro terpenoid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity Inferred from electronic annotation. Source: HAMAP ATP binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 299	299	4-diphosphocytidyl-2-C-methyl-D-erythritol kinase HAMAP MF_00061		PRO_0000189191
Regions
	Nucleotide binding	94 – 104	11	ATP Potential
Sites
	Active site	11	1	By similarity
	Active site	136	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WNY5-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 8B01D623620C0A91	FASTA	299	31,897
	10 20 30 40 50 60 MTLYDVPAPA KLNLFLHVVG RRADGYHLLQ TAFRFIDLAD TLHFEARADG AIGRAYELPG 70 80 90 100 110 120 VAESDDLVVR AARSLQRATG TRQGAQIGLH KRIPQGGGLG GGSSDAATTL IALNRLWGTG 130 140 150 160 170 180 LSRSQLMQLA LPLGADVPVF VFGQSAFAQG VGEDLTAVAL PPAAYLVVQP DAGVPTAAIF 190 200 210 220 230 240 SDPDLTRDCA SVTIADFLAL PTFCFGRNDL EPVVLRRYPE VSGAVRWLFE HGLRVRMSGS 250 260 270 280 290 GACLFAEFPT LPEAVLAQEE ITATMRVAGK TTSHTHPGFR LVQASTGLTE HPLRNWIAS

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640439 Genomic DNA. Translation: CAE31399.1.
RefSeq	NP_887449.1.
3D structure databases
SMR	Q7WNY5. Positions 5-261.
ModBase	Search...
Genome annotation databases
GeneID	2663204.
KEGG	bbr:BB0900.
NMPDR	fig|257310.1.peg.896.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG734593.
OMA	LNLFLHV.
PhylomeDB	Q7WNY5.
Enzyme and pathway databases
BioCyc	BBRO257310:BB0900-MONOMER.
BRENDA	2.7.1.148. 413.
Family and domain databases
HAMAP	MF_00061. IspE. [Tree]
InterPro	IPR006204. GHMP_kinase. IPR013750. GHMP_kinase_C. IPR004424. IspE. IPR020568. Ribosomal_S5_D2-typ_fold. IPR014721. Ribosomal_S5_D2-typ_fold_subgr. [Graphical view]
Gene3D	G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
PANTHER	PTHR20861:SF2. IspE. 1 hit.
Pfam	PF08544. GHMP_kinases_C. 1 hit. PF00288. GHMP_kinases_N. 1 hit. [Graphical view]
PIRSF	PIRSF010376. IspE. 1 hit.
TIGRFAMs	TIGR00154. ispE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ISPE_BORBR

Accession

Primary (citable) accession number: Q7WNY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)