Reviewed, UniProtKB/Swiss-Prot A9IS87 (ISPDF_BART1)

Names and origin

Protein names

Recommended name:
    Bifunctional enzyme ispD/ispF
Including the following 2 domains:
    1- Recommended name:
            2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
              EC=2.7.7.60
        Alternative name(s):
            4-diphosphocytidyl-2C-methyl-D-erythritol synthase
            MEP cytidylyltransferase
              Short name=MCT
    2- Recommended name:
            2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
                Short name=MECPS
                Short name=MECDP-synthase
              EC=4.6.1.12

Gene names

Name:	ispDF
Ordered Locus Names:	BT_0870

Organism

Bartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]

Taxonomic identifier

382640 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (ispD), and converts 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate into 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) and CMP (ispF) By similarity.
Catalytic activity	CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. HAMAP MF_01520 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP. HAMAP MF_01520
Cofactor	Divalent metal cations By similarity.
Pathway	Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. HAMAP MF_01520 Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Sequence similarities	In the N-terminal section; belongs to the ispD family. In the C-terminal section; belongs to the ispF family.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Ligand	Metal-binding
Molecular function	Lyase Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	terpenoid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity Inferred from electronic annotation. Source: HAMAP 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 398	398	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000333304
Regions
	Region	1 – 237	237	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	238 – 398	161	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	244	1	Divalent metal cation By similarity
	Metal binding	246	1	Divalent metal cation By similarity
	Metal binding	278	1	Divalent metal cation By similarity
	Site	17	1	Transition state stabilizer By similarity
	Site	26	1	Transition state stabilizer By similarity
	Site	156	1	Positions MEP for the nucleophilic attack By similarity
	Site	213	1	Positions MEP for the nucleophilic attack By similarity
	Site	270	1	Transition state stabilizer By similarity
	Site	369	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9IS87-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: FB2BA67BCCE22EC0	FASTA	398	44,458
	10 20 30 40 50 60 MSISIAAIIL AAGRGERAGS PHKIPKQYRL LGKKPIIYHT VCRFLRHPAI TTIILVIHPE 70 80 90 100 110 120 DRQICEQALA EFKERFIIVE GGSTRQISTL HGLQALKKFN PQYVHIHDGA RPFIENELLD 130 140 150 160 170 180 NIHNTLTPQE GVLPVLPISD TLKRVNHQYV LETIPRTHLY SAQTPQCFPF EPILAAHKQA 190 200 210 220 230 240 KRVCKEDFTD DCAIAEWFGL PMRTIPGDPH NIKITWHKDF DTAHLYLQKK MQMFPDIRVG 250 260 270 280 290 300 NGYDVHSFEE GDFLILCGIR IPFHKKLNGH SDADVALHAL TDALLATRGA GDIGTHFPPS 310 320 330 340 350 360 DPQWKNVSSE IFLRHALSLL KQAGGRIANV DITVIAENPK IGPYRHAMIE NLMTILAITP 370 380 390 DRISIKATTN ERLGFIGRGE GIAALATASV LYPGEIPQ

References

[1]

"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors." Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C. Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM260525 Genomic DNA. Translation: CAK01274.1.
RefSeq	YP_001609269.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5829986.
GenomeReviews	Gene locus BT_0870 in contig AM260525_GR.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	IVLIHDA.
Family and domain databases
HAMAP	MF_01520. [Tree]
InterPro	IPR001228. ISPD_synthase. IPR018294. ISPD_synthase_CS. IPR003526. MECDP_synthase_core. IPR020555. MECDP_synthase_CS. [Graphical view]
Gene3D	G3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit.
Pfam	PF01128. IspD. 1 hit. PF02542. YgbB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00453. ispD. 1 hit. TIGR00151. ispF. 1 hit.
PROSITE	PS01295. ISPD. False negative. PS01350. ISPF. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ISPDF_BART1

Accession

Primary (citable) accession number: A9IS87

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	November 3, 2009
This is version 15 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)