Reviewed, UniProtKB/Swiss-Prot Q9HVA2 (ILVC_PSEAE)

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
Ordered Locus Names:	PA4694

Organism

Pseudomonas aeruginosa [Complete proteome] [HAMAP]

Taxonomic identifier

287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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
Technical term	3D-structure Complete proteome
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 – 338

338

Ketol-acid reductoisomerase HAMAP MF_00435

PRO_0000151342

Sites

Active site

107

1

Potential

Secondary structure

1

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338

Helix Strand Turn

Details...

Helix

6 – 8

3

Helix

11 – 15

5

Beta strand

19 – 22

4

Helix

26 – 37

12

Beta strand

42 – 45

4

Helix

51 – 58

8

Beta strand

62 – 64

3

Helix

66 – 71

6

Beta strand

74 – 78

5

Helix

82 – 92

11

Helix

94 – 96

3

Beta strand

102 – 106

5

Helix

109 – 112

4

Beta strand

123 – 131

9

Helix

134 – 141

8

Beta strand

148 – 154

7

Beta strand

156 – 158

3

Helix

160 – 170

11

Helix

173 – 176

4

Beta strand

178 – 180

3

Helix

183 – 196

14

Turn

197 – 199

3

Helix

200 – 215

16

Helix

220 – 227

8

Turn

228 – 230

3

Helix

231 – 249

19

Helix

252 – 265

14

Helix

268 – 282

15

Helix

285 – 295

11

Helix

299 – 310

12

Helix

312 – 321

10

Sequences

	Sequence		Length	Mass (Da)
	Q9HVA2-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 93CF5F7DA9F61B0A	FASTA	338	36,425
	10 20 30 40 50 60 MRVFYDKDCD LSIIQGKKVA IIGYGSQGHA HACNLKDSGV DVTVGLRSGS ATVAKAEAHG 70 80 90 100 110 120 LKVADVKTAV AAADVVMILT PDEFQGRLYK EEIEPNLKKG ATLAFAHGFS IHYNQVVPRA 130 140 150 160 170 180 DLDVIMIAPK APGHTVRSEF VKGGGIPDLI AIYQDASGNA KNVALSYACG VGGGRTGIIE 190 200 210 220 230 240 TTFKDETETD LFGEQAVLCG GCVELVKAGF ETLVEAGYAP EMAYFECLHE LKLIVDLMYE 250 260 270 280 290 300 GGIANMNYSI SNNAEYGEYV TGPEVINAES RAAMRNALKR IQDGEYAKMF ITEGAANYPS 310 320 330 MTAYRRNNAA HPIEQIGEKL RAMMPWIAAN KIVDKSKN

References

[1]

"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE004091 Genomic DNA. Translation: AAG08080.1.

PIR

E83059.

RefSeq

NP_253382.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NP3	X-ray	2.00	A/B/C/D	1-338	[»]

ModBase

Search...

Genome annotation databases

GeneID

881483.

GenomeReviews

Gene locus PA4694 in contig AE004091_GR.

KEGG

pae:PA4694.

Organism-specific databases

PseudoCAP

PA4694.

CMR

Search...

Phylogenomic databases

HOGENOM

Q9HVA2.

OMA

Q9HVA2. AHGFNIR.

Enzyme and pathway databases

BioCyc

PAER208964:PA4694-MON.

BRENDA

1.1.1.86. 354.

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_PSEAE

Accession

Primary (citable) accession number: Q9HVA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 58 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)