A8MHH5 (DXR_ALKOO) 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:	Clos_1519

Organism

Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) [Complete proteome] [HAMAP]

Taxonomic identifier

350688 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Alkaliphilus

Protein attributes

Sequence length	381 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 – 381	381	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000058411
Regions
	Nucleotide binding	7 – 36	30	NADP By similarity
Sites
	Metal binding	147	1	Divalent metal cation By similarity
	Metal binding	149	1	Divalent metal cation By similarity
	Metal binding	218	1	Divalent metal cation By similarity
	Binding site	122	1	Substrate By similarity
	Binding site	149	1	Substrate By similarity
	Binding site	173	1	Substrate By similarity
	Binding site	196	1	Substrate By similarity
	Binding site	218	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8MHH5 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: 9716DB6257C55CA5	FASTA	381	42,523
	10 20 30 40 50 60 MKNISILGST GSIGTQTLDV VRNHPEKFKI VALSASGNID AIENQIHEFH PEIVAVFHRE 70 80 90 100 110 120 KAEILSARIG KKVKVVSGIE GLIEVATLDS ADIVVTSVVG SIGLIPTVEA IRCGKTIALA 130 140 150 160 170 180 NKETLVVAGE LIKKEAEKHK VQIIPVDSEH SAIFQCLQGE DIHNISRIIL TASGGAFRNW 190 200 210 220 230 240 EKQDIQHAKA QDALKHPTWN MGSKVTIDSA SLMNKGLEVM EARWLFNVEL DKIDVIVHPQ 250 260 270 280 290 300 SIVHSMVEYN DFSIIAQIGA PDMRGPIQYA LSYPNRINSS IERLDFRKIS ALTFMAPDTD 310 320 330 340 350 360 KFPCLSLAYE SLKIGKTMPC VLNGANEVLV EYFLEDRIGF YDIPKFIEKA MSAHKPWVYT 370 380 DIEELLEVDR WVRNWIKEQI E

References

[1]

"Complete genome of Alkaliphilus oremlandii OhILAs." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OhILAs.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000853 Genomic DNA. Translation: ABW19062.1.
RefSeq	YP_001513058.1. NC_009922.1.
3D structure databases
ProteinModelPortal	A8MHH5.
ModBase	Search...
Protein-protein interaction databases
STRING	A8MHH5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5676959.
GenomeReviews	Gene locus Clos_1519 in contig CP000853_GR.
KEGG	aoe:Clos_1519.
PATRIC	20868266. VBIAlkOre124042_1589.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG430762.
OMA	IHSMVEY.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	AORE350688:CLOS_1519-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_ALKOO

Accession

Primary (citable) accession number: A8MHH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	December 4, 2007
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program