[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Wernegreen J.J., Moran N.A.; "Accelerated evolutionary rates at biosynthetic loci of Buchnera-Uroleucon."; Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.

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

AF217554; AAK01025.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q9AQ99; 1-345.

ModBase

Q9AQ99.

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.
IPR000506; AcH_isomrdctse_C.
IPR013116; IlvN.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR21371; AcH_isomrdctse; 1.

Pfam

PF01450; IlvC; 1.
PF07991; IlvN; 1.
Pfam graphical view of domain structure.

TIGR00465; ilvC; 1.

Other

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >345`	`>345`	`Ketol-acid reductoisomerase.`	`PRO_0000151296`
`ACT_SITE`	`65 65`		`Potential.`
`NON_TER`	`1 1`
`NON_TER`	`345 345`

Sequence information

Length: 345 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 39244 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 6FE05ABA7849DD03 [This is a checksum on the sequence]

        10         20         30         40         50         60 
KKNSIAKKNQ SWINAIENNF KVDDYESLIP NADLVINLTP DKEHHHVVQV LQKLMKKNSC 

        70         80         90        100        110        120 
LGYSHGFNIV EFGEIIRKDI TVIMVAPKCP GTEVREEYKR GFGVPTLIAV HNENDIRQIG 

       130        140        150        160        170        180 
LDIAKAWSFS IGSHRAGVLE SSFIAEVKSD LMGEQTILCG MLQTASLLCY EKLIANKNDP 

       190        200        210        220        230        240 
AYASKLIQNG WETITESLKH GGITLMMDRL SNASKIRAYN ISEKIKKILS SLFQKHMNDI 

       250        260        270        280        290        300 
ISGEFSHKMM QDWQNNNKQL LDWRNKNKNT SFEKAPVYHN KIPEQEYYDH GILMIAILKA 

       310        320        330        340 
GIELSFETML NSGIIAESAY YESLHELPLI ANTIARKKLY EMNKV

Q9AQ99 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