NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).

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.
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 .
SIMILARITY: Belongs to the DXR family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000040; BAC50120.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_771495.1; -.

3D structure databases

HSSP

P45568; 1K5H. [HSSP ENTRY / PDB]

ModBase

Q89KP9.

Enzyme and pathway databases

BioCyc

BJAP224911:BLL4855-MON; -.

Ontologies

GO:0030604;	Molecular function: 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity (inferred from electronic annotation from HAMAP).
GO:0046872;	Molecular function: metal ion binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0016114;	Biological process: terpenoid biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00183; -; 1.
PBIL [Tree]

InterPro

IPR003821; DXP_reductoisomerase.
IPR013644; DXP_reductoisomerase_C.
IPR013512; DXP_reductoisomerase_N.
Graphical view of domain structure.

Pfam

PF08436; DXP_redisom_C; 1.
PF02670; DXP_reductoisom; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF006205; Dxp_reductismrs; 1.

TIGR00243; Dxr; 1.

Genome annotation databases

GeneID

1052114; -.

GenomeReviews

BA000040_GR; bll4855.

KEGG

bja:bll4855; -.

NMPDR

fig|224911.1.peg.4855; -.

Phylogenomic databases

HOGENOM

Q89KP9; -.

Genome annotation databases

CMR

Q89KP9; bll4855.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 407`	`407`	`1-deoxy-D-xylulose 5-phosphate reductoisomerase.`	`PRO_0000163621`
`NP_BIND`	`22 51`	`30`	`NADP (By similarity).`
`METAL`	`162 162`		`Divalent metal cation (By similarity).`
`METAL`	`164 164`		`Divalent metal cation (By similarity).`
`METAL`	`233 233`		`Divalent metal cation (By similarity).`
`BINDING`	`137 137`		`Substrate (By similarity).`
`BINDING`	`164 164`		`Substrate (By similarity).`
`BINDING`	`188 188`		`Substrate (By similarity).`
`BINDING`	`211 211`		`Substrate (By similarity).`
`BINDING`	`233 233`		`Substrate (By similarity).`

Sequence information

Length: 407 AA [This is the length of the unprocessed precursor]

Molecular weight: 42699 Da [This is the MW of the unprocessed precursor]

CRC64: F1202A78BB89D0C6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSAVPLRNNK AAASAVRSVT VLGATGSIGD STMDLLRASP ERYRVEALTA NGNVEALAKL 

        70         80         90        100        110        120 
AKEFSARFVA IADTSKFAEL KAALAGTSTE CGAGESAVIE AGARPADWVM AAVSGAAGLK 

       130        140        150        160        170        180 
PALAAVDRGA HVALANKECL VCAGDFFMQR AAKAGACILP ADSEHNALFQ ALGSGNRDEL 

       190        200        210        220        230        240 
VRVIITASGG PFRTWKPADI EQATLAQALK HPNWSMGQKI TIDSASMMNK GLEVIEASYL 

       250        260        270        280        290        300 
FALSPDEIDV LVHPQSIIHG MVEFSDRSVV AQLGSPDMRT PIAHCLGWPD RIKGPAAKLD 

       310        320        330        340        350        360 
LAKIGQLTFE APDFERFPGL RLAYDSLRTG KGATTVYNAA NEVAVAAFIA GKIRFGAIAR 

       370        380        390        400 
LVEATLEDWI RGGNQTPLTS ADDAISVDHV ARNRAAALLP QIALKAS

Q89KP9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools