Reviewed, UniProtKB/Swiss-Prot Q9AQ99 (ILVC_BUCUN)

Names and origin

Protein names

Recommended name:
    Ketol-acid reductoisomerase
    EC=1.1.1.86
Alternative name(s):
    Acetohydroxy-acid isomeroreductase
    Alpha-keto-beta-hydroxylacil reductoisomerase

Gene names

Name:

ilvC

Organism

Buchnera aphidicola subsp. Uroleucon sonchi

Taxonomic identifier

118118 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	345 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	(R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. HAMAP MF_00435 (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. HAMAP MF_00435
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. HAMAP MF_00435 Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. HAMAP MF_00435
Sequence similarities	Belongs to the ketol-acid reductoisomerase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	isoleucine biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW valine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	binding Inferred from electronic annotation. Source: InterPro ketol-acid reductoisomerase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›345	›345	Ketol-acid reductoisomerase HAMAP MF_00435		PRO_0000151296
Sites
	Active site	65	1	Potential
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	345	1

Sequences

	Sequence		Length	Mass (Da)
	Q9AQ99-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 6FE05ABA7849DD03	FASTA	345	39,244
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF217554 Genomic DNA. Translation: AAK01025.1.
3D structure databases
SMR	Q9AQ99. Positions 1-345.
ModBase	Search...
Family and domain databases
HAMAP	MF_00435. [Tree]
InterPro	IPR013023. AcH_isomrdctse. IPR000506. AcH_isomrdctse_C. IPR013116. IlvN. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR21371. AcH_isomrdctse. 1 hit.
Pfam	PF01450. IlvC. 1 hit. PF07991. IlvN. 1 hit. [Graphical view]
TIGRFAMs	TIGR00465. ilvC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ILVC_BUCUN

Accession

Primary (citable) accession number: Q9AQ99

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)