Q6HG59 (DXR1_BACHK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1-deoxy-D-xylulose 5-phosphate reductoisomerase 1
Short name=DXP reductoisomerase 1
EC=1.1.1.267

Alternative name(s):
1-deoxyxylulose-5-phosphate reductoisomerase 1
2-C-methyl-D-erythritol 4-phosphate synthase 1

Gene names

Name:	dxr1
Ordered Locus Names:	BT9727_3144

Organism

Bacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]

Taxonomic identifier

281309 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	385 AA.
Sequence status	Complete.
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. HAMAP MF_00183
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. HAMAP MF_00183
Pathway	Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate 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	isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-deoxy-D-xylulose-5-phosphate reductoisomerase activity Inferred from electronic annotation. Source: EC NADPH binding Inferred from electronic annotation. Source: InterPro 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 – 385	385	1-deoxy-D-xylulose 5-phosphate reductoisomerase 1 HAMAP MF_00183		PRO_0000163611
Regions
	Nucleotide binding	8 – 37	30	NADP By similarity
Sites
	Metal binding	148	1	Divalent metal cation By similarity
	Metal binding	150	1	Divalent metal cation By similarity
	Metal binding	219	1	Divalent metal cation By similarity
	Binding site	123	1	Substrate By similarity
	Binding site	150	1	Substrate By similarity
	Binding site	174	1	Substrate By similarity
	Binding site	197	1	Substrate By similarity
	Binding site	219	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6HG59 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 65DA0CDC461F8AA3	FASTA	385	42,546
	10 20 30 40 50 60 MVKYISILGS TGSIGTSALD VVSAHPEHFK IVGLTANYNI ELLEQQIKTF QPRIVSVATK 70 80 90 100 110 120 ELADTLRTRI STNTKITYGT DGLIAVATHP NSNLVLSSVV GVSGLLPTIE ALKAKKDIAI 130 140 150 160 170 180 ANKETLVAAG HIVTELAKQN GCRLIPVDSE HSAIFQCLNG ENNKEIDKLI VTASGGAFRD 190 200 210 220 230 240 KTREEMKTLQ AKDALKHPNW LMGAKLTIDS ATLMNKGFEV MEARWLFDIP YEKIDVMIHK 250 260 270 280 290 300 ESIIHSLVEF IDGSVIAQLG APDMRMPIQY AFHYPTRLPS SYEKLNLLEI GSLHFEKPDL 310 320 330 340 350 360 EKFPCLQYAY ECGKIGGTTP AVLNAANEIA NALFLKNEIA FFDIEKTIYK TVEAHHNVKD 370 380 PSLDAILEAD QWARQYANQL LIKKS

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT62181.1.
RefSeq	YP_037467.1. NC_005957.1.
3D structure databases
ProteinModelPortal	Q6HG59.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000075147; EBBACP00000073233; EBBACG00000075138.
GeneID	2857981.
GenomeReviews	Gene locus BT9727_3144 in contig AE017355_GR.
KEGG	btk:BT9727_3144.
NMPDR	fig|281309.1.peg.3107.
PATRIC	18987242. VBIBacThu119411_3347.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000001768.
HOGENOM	HBG430762.
OMA	IAKLYIT.
ProtClustDB	PRK12464.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_3144-MONOMER.
Family and domain databases
HAMAP	MF_00183. DXP_reductoisom. [Tree]
InterPro	IPR003821. DXP_reductoisomerase. IPR013644. DXP_reductoisomerase_C. IPR013512. DXP_reductoisomerase_N. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00099.
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

DXR1_BACHK

Accession

Primary (citable) accession number: Q6HG59

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program