[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(92)90018-K; PubMed=1398116 [NCBI, ExPASy, EBI, Israel, Japan] Sista H., Bowman B.; "Characterization of the ilv-2 gene from Neurospora crassa encoding alpha-keto-beta-hydroxylacyl reductoisomerase."; Gene 120:115-118(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; DOI=10.1093/nar/gkg293; PubMed=12655011 [NCBI, ExPASy, EBI, Israel, Japan] Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.; "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."; Nucleic Acids Res. 31:1944-1954(2003).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; DOI=10.1038/nature01554; PubMed=12712197 [NCBI, ExPASy, EBI, Israel, Japan] Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.; "The genome sequence of the filamentous fungus Neurospora crassa."; Nature 422:859-868(2003).

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.
COFACTOR: Magnesium.
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 .
SUBCELLULAR LOCATION: Mitochondrion.
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

M84189; AAB00797.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL670005; CAD21284.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AABX02000011; EAA32099.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC1428; JC1428.

RefSeq

XP_961335.1; -.

3D structure databases

HSSP

Q9HVA2; 1NP3. [HSSP ENTRY / PDB]

ModBase

P38674.

Enzyme and pathway databases

BioCyc

NCRA-XX3-01:NCRA-XX3-01-007356-MON; -.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0050662;	Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0004455;	Molecular function: ketol-acid reductoisomerase activity (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009082;	Biological process: branched chain family amino acid biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013023; AcH_isomrdctse.
IPR000506; AcH_isomrdctse_C.
IPR013328; DHase_multihelical.
IPR013116; IlvN.
IPR016207; KetolA_reductoisomerase_fun.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

PANTHER

PTHR21371; AcH_isomrdctse; 1.

Pfam

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

PIRSF

PIRSF000119; Ilv5_fungal; 1.

TIGRFAMs

TIGR00465; ilvC; 1.

ProtoNet

P38674.

Genome annotation databases

GeneID

3877517; -.

KEGG

ncr:NCU03608; -.

NMPDR

fig|5141.1.peg.843; -.

Other

UniRef

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

Keywords

Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; Magnesium; Mitochondrion; NADP; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 26`	`26`	`Mitochondrion (Potential).`
`CHAIN`	`27 402`	`376`	`Ketol-acid reductoisomerase, mitochondrial.`	`PRO_0000015632`
`NP_BIND`	`90 99`	`10`	`NADP (Potential).`
`ACT_SITE`	`177 177`		`Potential.`
`CONFLICT`	`358 358`		`T -> R (in Ref. 1; AAB00797).`
`CONFLICT`	`392 393`		`Missing (in Ref. 1; AAB00797).`

Sequence information

Length: 402 AA [This is the length of the unprocessed precursor]

Molecular weight: 44623 Da [This is the MW of the unprocessed precursor]

CRC64: 246F795898D2A174 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAARNCTKAL RPLARQLATP AVQRRTFVAA ASAVRASVAV KAVAAPARQQ VRGVKTMDFA 

        70         80         90        100        110        120 
GHKEEVHERA DWPAEKLLDY FKNDTLALIG YGSQGHGQGL NLRDNGLNVI VGVRKNGKSW 

       130        140        150        160        170        180 
EDAIQDGWVP GKNLFDVDEA ISRGTIVMNL LSDAAQSETW PHIKPQITKG KTLYFSHGFS 

       190        200        210        220        230        240 
PVFKDLTKVE VPTDVDVILV APKGSGRTVR SLFREGRGIN SSFAVYQDVT GKAKEKAVAL 

       250        260        270        280        290        300 
GVAVGSGYLY ETTFEKEVYS DLYGERGCLM GGIHGMFLAQ YEVLRERGHS PSEAFNETVE 

       310        320        330        340        350        360 
EATQSLYPLI GAHGMDWMFD ACSTTARRGA IDWTPKFKDA LKPVFNNLYD SVKNGDETKR 

       370        380        390        400 
SLEYNSQPDY RERYEAELDE IRNLEIWRAG KAVRSLRPEN QK

P38674 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