Q8KG43 (DXR_CHLTE) Reviewed, UniProtKB/Swiss-Prot

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:	CT0125

Organism

Chlorobium tepidum

Taxonomic identifier

1097 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum

Protein attributes

Sequence length	382 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 Reference 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 – 382	382	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163634
Regions
	Nucleotide binding	7 – 36	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)
	Q8KG43 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 4B42A8B6F36368CA	FASTA	382	41,344
	10 20 30 40 50 60 MKSLSILGST GSIGLSTLDV VRRHPERFSI AALAEGHDVE MLLKQIDEFR PSLVSVRDEA 70 80 90 100 110 120 SRERLKGMLG DHKPEILCGL EGAAEVAAVD GADMVVSAIV GAAGLVPTVR AIEAGKDIAL 130 140 150 160 170 180 ANKETLVVAG QLVSDLVKKH DVKLLPVDSE HSAIFQSLVG HRTEDIERII LTASGGPFRK 190 200 210 220 230 240 TPAEELKNVG PEQALKHPQW SMGAKITIDS ATLMNKGLEV IEAHWLFDMP AEKIGVVVHP 250 260 270 280 290 300 QSIIHSMVEY IDGCVIAQLG VPDMRAPIAY ALAWPERCET GIGKLDLTKV ATLTFEEPDM 310 320 330 340 350 360 ERFPALRLAF DALKAGQTYP AVLNAANEIA VAAFLDKKIG FTDIAGTVDK TMQAHEAWTP 370 380 ITLEEYLQAD KWARETARQL IG

References

[1]

"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. , Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed: 12093901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006470 Genomic DNA. Translation: AAM71373.1.
RefSeq	NP_661031.1. NC_002932.3.
3D structure databases
ProteinModelPortal	Q8KG43.
SMR	Q8KG43. Positions 2-381.
ModBase	Search...
Proteomic databases
PRIDE	Q8KG43.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1006807.
GenomeReviews	Gene locus CT0125 in contig AE006470_GR.
KEGG	cte:CT0125.
NMPDR	fig|194439.1.peg.125.
PATRIC	21398349. VBIChlTep116050_0123.
TIGR	CT0125.
Phylogenomic databases
HOGENOM	HBG430762.
OMA	IHSMVEY.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	CTEP194439:CT_0125-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

DXR_CHLTE

Accession

Primary (citable) accession number: Q8KG43

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program