NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/ng.2007.38; PubMed=18037886 [NCBI, ExPASy, EBI, Israel, Japan]
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors.";
Nat. Genet. 39:1469-1476(2007).

Comments

CATALYTIC ACTIVITY: (R)-2,3-dihydroxy-3-methylbutanoate + NADP⁺ = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP⁺ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4 .
PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4 .
SIMILARITY: Belongs to the ketol-acid reductoisomerase 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

AM260525; CAK01894.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001609889.1; -.

3D structure databases

ModBase

A9IW67.

Ontologies

GO:0004455;	Molecular function: ketol-acid reductoisomerase activity (inferred from electronic annotation from HAMAP).
GO:0009097;	Biological process: isoleucine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0009099;	Biological process: valine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00435; -; 1.
PBIL [Tree]

InterPro

IPR013023; AcH_isomrdctse.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR21371; AcH_isomrdctse; 1.

TIGRFAMs

TIGR00465; ilvC; 1.

BLOCKS

A9IW67.

Genome annotation databases

GeneID

5829529; -.

GenomeReviews

AM260525_GR; BT1549.

CMR

A9IW67; BT1549.

Other

ProtoNet

A9IW67.

UniRef

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

Keywords

Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 339`	`339`	`Ketol-acid reductoisomerase.`	`PRO_1000080618`
`ACT_SITE`	`108 108`		`Potential.`

Sequence information

Length: 339 AA [This is the length of the unprocessed precursor]

Molecular weight: 37279 Da [This is the MW of the unprocessed precursor]

CRC64: CF15CF243932015D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRVYYDRDAD MNLIKGKKVA IVGYGSQGRA HALNLKDSGV QNVQIALRSG SETVKKATAD 

        70         80         90        100        110        120 
GFEVVSVAEA AKWADLIMMA TPDELQADIY KEHIHDHLRD GAAVAFAHGL SIHFGLIEPK 

       130        140        150        160        170        180 
KTVDVVMIAP KGPGHTVRHE YQRGCGVPCL IAVAQDASGH AHSVALSYAC GLGGGRAGVI 

       190        200        210        220        230        240 
ETTFKEECET DLFGEQAVLC GGLVELIRAG YETLTQAGYA PEMAYFECLH EVKLIVDLMY 

       250        260        270        280        290        300 
EGGISNMNYS ISNTAEWGEY MSGPRVITDE TRAEMKRILK DIQTGKFTSN WIQEYKAGAA 

       310        320        330 
HFKSMRRLND NHPIEEVGKK LRSMMPWIKS NALVDKERN

A9IW67 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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