NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
"Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium caulinodans ORS571.";
Submitted (APR-2007) 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

AP009384; BAF88372.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001525290.1; -.

3D structure databases

ModBase

A8I679.

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.

TIGRFAMs

TIGR00465; ilvC; 1.

BLOCKS

A8I679.

Genome annotation databases

GeneID

5690176; -.

GenomeReviews

AP009384_GR; AZC_2374.

CMR

A8I679; AZC_2374.

Other

ProtoNet

A8I679.

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_1000072319`
`ACT_SITE`	`108 108`		`Potential.`

Sequence information

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

Molecular weight: 37152 Da [This is the MW of the unprocessed precursor]

CRC64: 919A66D1C1332F2A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRVYYDRDAD LNLIKGKKVV IVGYGSQGHA HALNLRDSGV KDIVVALRPG SASAKKAEGE 

        70         80         90        100        110        120 
GFKVMTPAEA AKWGDVVMML TPDELQADIY RESLHDNMKQ GAALLFAHGL NVHFNLIEPR 

       130        140        150        160        170        180 
KDLDVLMIAP KGPGHTVRSE YQRGGGVPTL IAIAQDASGN AHDLGLSYAS ANGGGRAGII 

       190        200        210        220        230        240 
ETTFKEECET DLFGEQVVLC GGLVELIRAG FETLVEAGYA PEMAYFECLH EVKLIVDLIY 

       250        260        270        280        290        300 
EGGIANMNYS ISNTAEYGEY VTGPRIITPE TKAEMKRVLT DIQTGKFTRD WMLENKVNQA 

       310        320        330 
SFKATRARHN AHQIEAVGEK LREMMPWIKA KALVDKSKN

A8I679 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