Reviewed, UniProtKB/Swiss-Prot Q7NVY8 (DXR_CHRVO)

Names and origin

Protein names

Recommended name:
    1-deoxy-D-xylulose 5-phosphate reductoisomerase
      Short name=DXP reductoisomerase
    EC=1.1.1.267
Alternative name(s):
    1-deoxyxylulose-5-phosphate reductoisomerase
    2-C-methyl-D-erythritol 4-phosphate synthase

Gene names

Name:	dxr
Ordered Locus Names:	CV_2202

Organism

Chromobacterium violaceum [Complete proteome] [HAMAP]

Taxonomic identifier

536 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) By similarity.
Catalytic activity	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. HAMAP MF_00183
Cofactor	Divalent cation By similarity.
Pathway	Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via DXP pathway; isopentenyl-PP from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP MF_00183
Sequence similarities	Belongs to the DXR family.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Ligand	Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW terpenoid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	1-deoxy-D-xylulose-5-phosphate reductoisomerase 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 – 394	394	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163635
Regions
	Nucleotide binding	10 – 39	30	NADP By similarity
Sites
	Metal binding	153	1	Divalent metal cation By similarity
	Metal binding	155	1	Divalent metal cation By similarity
	Metal binding	229	1	Divalent metal cation By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	184	1	Substrate By similarity
	Binding site	207	1	Substrate By similarity
	Binding site	229	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7NVY8-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 482DEAA31A2275F0	FASTA	394	41,674
	10 20 30 40 50 60 MTKPQGIAVL GATGSVGCNT LDVVARHPER YRVVALTAHR QLDKLFEQAR RFCPDYLVVA 70 80 90 100 110 120 DADAAARLRA RLAEAGLRSE VLHGADALVQ VAALPEVDAV MASIVGAAGL PSALAAARAG 130 140 150 160 170 180 KRILLANKES LVVAGRLFMD AVRASGSALL PVDSEHSAIF QSLPADYAGN PDGAGVRKII 190 200 210 220 230 240 LTASGGPFRN RPAADLAHVT PDEACRHPNW SMGRKISVDS ATLMNKGLEV IEARWLFNVP 250 260 270 280 290 300 PSRIEVAVHP QSVIHSMVQY RDGSVMAQLG SPDMRTPIAC ALAWPERIDA GVEPMDFFSL 310 320 330 340 350 360 SDLTFEKPDL ERFPCLQLAF DALEMGGDAP AVLNAANEVA VAAFLAGRLR FVDIPRVVAA 370 380 390 SLSGVSCAAS DSLEGLLARD EEARRFAEGG VAAC

References

[1]

"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability." Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G. Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016825 Genomic DNA. Translation: AAQ59875.1.
RefSeq	NP_901872.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2549212.
GenomeReviews	Gene locus CV_2202 in contig AE016825_GR.
KEGG	cvi:CV_2202.
NMPDR	fig|243365.1.peg.2202.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7NVY8.
OMA	Q7NVY8. IHSMVEY.
Enzyme and pathway databases
BioCyc	CVIO243365:CV_2202-MON.
BRENDA	1.1.1.267. 415.
Family and domain databases
HAMAP	MF_00183. [Tree]
InterPro	IPR003821. DXP_reductoisomerase. IPR013644. DXP_reductoisomerase_C. IPR013512. DXP_reductoisomerase_N. [Graphical view]
Pfam	PF08436. DXP_redisom_C. 1 hit. PF02670. DXP_reductoisom. 1 hit. [Graphical view]
PIRSF	PIRSF006205. Dxp_reductismrs. 1 hit.
TIGRFAMs	TIGR00243. Dxr. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DXR_CHRVO

Accession

Primary (citable) accession number: Q7NVY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	December 15, 2003
Last modified:	June 16, 2009
This is version 39 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)