[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=10555290 [NCBI, ExPASy, EBI, Israel, Japan] Clark M.A., Moran N.A., Baumann P.; "Sequence evolution in bacterial endosymbionts having extreme base compositions."; Mol. Biol. Evol. 16:1586-1598(1999).

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

AF130813; AAF13803.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q9HVA2; 1NP3. [HSSP ENTRY / PDB]

ModBase

Q9RQ51.

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.
IPR014359; KetolA_reductoisomerase_bac.
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.

PIRSF

PIRSF000116; IlvC_gammaproteo; 1.

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`	`1 489`	`489`	`Ketol-acid reductoisomerase.`	`PRO_0000151292`
`ACT_SITE`	`131 131`		`Potential.`

Sequence information

Length: 489 AA [This is the length of the unprocessed precursor]

Molecular weight: 55710 Da [This is the MW of the unprocessed precursor]

CRC64: BFB94B15F507641F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNYFNSLNFR QKLINLRKCK LVEKNFFSKK CDILKRKNIV IVGCGSQGLN QGLNMRDSGL 

        70         80         90        100        110        120 
HVSYALRGSS ILNKNKSWEN ATKNNFFVDT YENIIPTADL VINLTPDKQR KEVVTLLQKF 

       130        140        150        160        170        180 
MKENSVLGFS HGFHIVEIGQ KIRNDITVIM VAPKCPGTEV REEYKKGFGV PSLIAVHMEN 

       190        200        210        220        230        240 
DPKKIGFEIA KAWAYSLGSH RAGVLHSSFI AEVKSDLMGE QTILCGMLQT SSLVCYDQLV 

       250        260        270        280        290        300 
SQGKDPNYAG KLIQLGWESI TESVKHGGIT LMLNRLSNTA KIRAYILSKK LKVMFSSLFR 

       310        320        330        340        350        360 
KHMDDIISGE FSKNMIDDWN SDDKKLKEWR TQIKKTDFEK CKICHKEISE QEYFDQGLLM 

       370        380        390        400        410        420 
VAILKAGIEL SFEIMVETGI KEESAYYESL HELPLIANTI ARKRLYEMNL VISDTAEYGS 

       430        440        450        460        470        480 
YLFSQSAIPL LKEFMNELCP GDLGEKISDL QFDNVTLNKI NHDIENHPVE IIGKKLRKYM 


VDMKPIKLS

Q9RQ51 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