Bifunctional enzyme IspD/IspF - Rhizobium loti (strain MAFF303099)

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Q98MX9 (ISPDF_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Bifunctional enzyme IspD/IspF

Including the following 2 domains:

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-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Short name=MECDP-synthase
Short name=MECPS
EC=4.6.1.12

Gene names

Name:	ispDF
Ordered Locus Names:	mll0395

Organism

Rhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]

Taxonomic identifier

266835 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
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. HAMAP MF_01520
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. HAMAP MF_01520
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: InterPro
Molecular function	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity Inferred from electronic annotation. Source: EC 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity Inferred from electronic annotation. Source: EC 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 – 407

407

Bifunctional enzyme IspD/IspF HAMAP MF_01520

PRO_0000075673

Regions

Region

1 – 246

246

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520

Region

247 – 407

161

2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding

253

Divalent metal cation By similarity

Metal binding

255

Divalent metal cation By similarity

Metal binding

287

Divalent metal cation By similarity

Site

Transition state stabilizer By similarity

Site

Transition state stabilizer By similarity

Site

165

Positions MEP for the nucleophilic attack By similarity

Site

222

Positions MEP for the nucleophilic attack By similarity

Site

279

Transition state stabilizer By similarity

Site

378

Transition state stabilizer By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q98MX9 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: FCEE6A5B4CD34F33
Show »

FASTA

407

42,834

        10         20         30         40         50         60 
MTEASENASA TGGVAVVIVA AGRGARAGQA NGPKQYQNIG GRAVIAHTLE IFLAHPRTDR 

        70         80         90        100        110        120 
IVVAIHADDH ELFRQAAGSQ AERVTAIIGG PTRQESVRLG LLALKEHAPG QVLIHDAVRP 

       130        140        150        160        170        180 
FVDADLIDRT ISAIGENEGA LPALPVADTL KRESAAGVVA ETVSRSGLHA AQTPQGFPYG 

       190        200        210        220        230        240 
PILAAHDKAF QLGRLDFTDD AAIAEWAHIP VKLVPGSPDN VKLTWARDIA MAHQRLSSER 

       250        260        270        280        290        300 
THFPDIRTGN GYDVHAFEPG DHVTLCGVAI PHDKKLSGHS DADVGLHALT DALLATCGAG 

       310        320        330        340        350        360 
DIGTHFPPSD PQWKGAASRI FVEHAAKVVR QRGGRIANAD ITLICEAPRV GPHREAMTAA 

       370        380        390        400 
LSRMLGISAD RISIKATTNE KLGFVGREEG IAAIATASVV FPGEVPE

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References

[1]

"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S.

Tabata S.
DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000012 Genomic DNA. Translation: BAB47984.1.
RefSeq	NP_102198.1. NC_002678.2.
3D structure databases
ProteinModelPortal	Q98MX9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1224861.
GenomeReviews	Gene locus mll0395 in contig BA000012_GR.
KEGG	mlo:mll0395.
NMPDR	fig\|266835.1.peg.303.
PATRIC	22474782. VBIMesLot2464_0313.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG672839.
OMA	IVLIHDA.
ProtClustDB	PRK09382.
Family and domain databases
HAMAP	MF_01520. IspDF. [Tree]
InterPro	IPR023423. IpsF_dom. IPR001228. ISPD_synthase. IPR018294. ISPD_synthase_CS. IPR003526. MECDP_synthase. IPR020555. MECDP_synthase_CS. [Graphical view]
Gene3D	G3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit.
KO	K12506.
Pfam	PF01128. IspD. 1 hit. PF02542. YgbB. 1 hit. [Graphical view]
SUPFAM	SSF69765. YgbB_synth. 1 hit.
TIGRFAMs	TIGR00453. IspD. 1 hit. TIGR00151. IspF. 1 hit.
PROSITE	PS01295. ISPD. 1 hit. PS01350. ISPF. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ISPDF_RHILO

Accession

Primary (citable) accession number: Q98MX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	October 1, 2001
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents