B2HJP9 (DXR_MYCMM) 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:	MMAR_1836

Organism

Mycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP]

Taxonomic identifier

216594 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	402 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 – 402	402	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000118493
Regions
	Nucleotide binding	18 – 47	30	NADP By similarity
Sites
	Metal binding	151	1	Divalent metal cation By similarity
	Metal binding	153	1	Divalent metal cation By similarity
	Metal binding	222	1	Divalent metal cation By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	153	1	Substrate By similarity
	Binding site	177	1	Substrate By similarity
	Binding site	200	1	Substrate By similarity
	Binding site	222	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B2HJP9 [UniParc]. Last modified June 10, 2008. Version 1. Checksum: B426D6B6D2AB8397	FASTA	402	41,796
	10 20 30 40 50 60 MTTATDGSAD GRLRVLVLGS TGSIGTQALE VIAANPDRFE VVGLAAGGSN LDTLLRQRAE 70 80 90 100 110 120 TGVTEIAIAD ERAAQLAGDI AYQGPDAVTR LVEETEADVV LNALVGALGL RPTLAALASG 130 140 150 160 170 180 ARLALANKES LVAGGPLVLQ AAQPGQIVPV DSEHSALAQC LRAGTPDEVA KLVLTASGGP 190 200 210 220 230 240 FRGWSAADLQ EVTPEQAGAH PTWSMGPMNT LNSASLVNKG LELIETHLLF GIPYERIEVV 250 260 270 280 290 300 VHPQSIVHSM VTFVDGSTIA QASPPDMKLP ISLALGWPRR VPGAARYCDF SQAQTWEFEP 310 320 330 340 350 360 LDDEVFPAVE LARHAGETGG CMTAVYNAAN EEAAAAFLAG RISFPAIVGT IADVLHAADQ 370 380 390 400 WAVSPANVDD VLDAQRWARQ RAQRAIAKAS PAGACEKVSG LA

References

[1]

"Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis." Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. , Mungall K., Norbertczak H., Quail M.A., Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T. Genome Res. 18:729-741(2008) [PubMed: 18403782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-535 / M.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000854 Genomic DNA. Translation: ACC40285.1.
RefSeq	YP_001850140.1. NC_010612.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	B2HJP9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000031810; EBMYCP00000030250; EBMYCG00000031805.
GeneID	6226095.
GenomeReviews	Gene locus MMAR_1836 in contig CP000854_GR.
KEGG	mmi:MMAR_1836.
PATRIC	18064563. VBIMycMar75906_1966.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000016490.
HOGENOM	HBG430762.
OMA	IHSMVEY.
ProtClustDB	PRK05447.
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_MYCMM

Accession

Primary (citable) accession number: B2HJP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	June 10, 2008
Last modified:	January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program