[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/PL00006760; PubMed=9516544 [NCBI, ExPASy, EBI, Israel, Japan] Clark M.A., Baumann L., Baumann P.; "Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon, gidA, and rho."; Curr. Microbiol. 36:158-163(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan] Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; "50 million years of genomic stasis in endosymbiotic bacteria."; Science 296:2376-2379(2002).

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

AF008210; AAC38126.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013218; AAM68109.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_660898.1; -.

3D structure databases

HSSP

Q9HVA2; 1NP3. [HSSP ENTRY / PDB]

ModBase

O51888.

Enzyme and pathway databases

BioCyc

BAPH198804:BUSG575-MON; -.

Ontologies

GO:0004455;	Molecular function: ketol-acid reductoisomerase activity (inferred from electronic annotation from HAMAP).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0009097;	Biological process: isoleucine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

TIGRFAMs

TIGR00465; ilvC; 1.

Genome annotation databases

GeneID

1005622; -.

GenomeReviews

AE013218_GR; BUsg_575.

KEGG

bas:BUsg575; -.

Phylogenomic databases

HOGENOM

O51888; -.

Genome annotation databases

CMR

O51888; BUsg_575.

Other

ProtoNet

O51888.

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`	`1 491`	`491`	`Ketol-acid reductoisomerase.`	`PRO_0000151287`
`ACT_SITE`	`131 131`		`Potential.`
`CONFLICT`	`36 36`		`N -> I (in Ref. 1; AAC38126).`

Sequence information

Length: 491 AA [This is the length of the unprocessed precursor]

Molecular weight: 56096 Da [This is the MW of the unprocessed precursor]

CRC64: E872D203A9A219E2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNYFNKLCFR KRINEIKKCR FMKENEFKNE NKILKNKKIV IVGCGSQGLN QALNMRDSGL 

        70         80         90        100        110        120 
NISFALKKNS ILRKNSSWLN ATKNNFEVND YESLIPNADL VINLTPDKQH ENVVKELQKL 

       130        140        150        160        170        180 
MKKNSCLGYS HGFNIVECGE IIRKDITVVM VAPKCPGTEV REEFKRGFGV PTLIAVHTEN 

       190        200        210        220        230        240 
DPKKIGLEIA KAWAFSTGGH RAGVLESSFI AEVKSDLMGE QTILCGLLQT ASLICYEKLI 

       250        260        270        280        290        300 
KDKHNPSYAA KLIQYGWETI TESLKHGGIT LMMDRLSNPS KIKAFKISKK IKKILSPLFK 

       310        320        330        340        350        360 
KHMDDIISGS FSKEMMIDWH NNDKKLLNWR EDTKKTPFEK NILSYSEKIS EQEYYDHGTL 

       370        380        390        400        410        420 
MVSILKSGIE LAFETMINTG IINESAYYES LHELPLIANT IARKKLYEMN IVISDTAEYG 

       430        440        450        460        470        480 
SYLFSEAAYP ILKDFIMSLE KNVLGLSLPN TKIDNIELYK INEEIRNHPI EIVGKKLRKH 

       490 
MKEMKSICVA K

O51888 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