P29107 (ILVC_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ketol-acid reductoisomerase
EC=1.1.1.86

Alternative name(s):
Acetohydroxy-acid isomeroreductase
Alpha-keto-beta-hydroxylacyl reductoisomerase

Gene names

Name:	ilvC
Ordered Locus Names:	sll1363

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › Synechocystis sp. PCC 6803

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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-Rule MF_00435 (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. HAMAP-Rule MF_00435
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. HAMAP-Rule MF_00435 Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. HAMAP-Rule MF_00435
Subunit structure	Homooctamer.
Sequence similarities	Belongs to the ketol-acid reductoisomerase family.
Caution	Was originally (Ref.2) isolated as a glutamyl-tRNA reductase.
Sequence caution	The sequence BAA18666.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	isoleucine biosynthetic process Inferred from electronic annotation. Source: HAMAP valine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	coenzyme 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
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 331	330	Ketol-acid reductoisomerase HAMAP-Rule MF_00435		PRO_0000151372
Sites
	Active site	108	1	Potential

Sequences

	Sequence		Length	Mass (Da)
	P29107 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 070C9D494F39CD44	FASTA	331	35,822
	10 20 30 40 50 60 MARMYYDQDA NLDLLAGKTV AIIGYGSQGH AHALNLKDSG VNVVVGLYSG SKSVAKAEGA 70 80 90 100 110 120 GLKVLSVAEA AKAADLIMIL LPDEVQKTVY EAEIAPNLVA GNVLLFAHGF NINFAQIVPP 130 140 150 160 170 180 ADVDVVMAAP KGPGHLVRRT YEQGQGVPAL FAVYQDASGQ ARDYAMAYAK GIGGTRAGIL 190 200 210 220 230 240 ETTFREETET DLFGEQVVLC GGLTALIKAG FDTLVEAGYQ PELAYFECLH EVKLIVDLIV 250 260 270 280 290 300 EGGLAKMRDS ISNTAEYGDL TRGPRIVTEE TKAEMRQILD EIQSGQFARE FVLENQAGKP 310 320 330 GFTAMRRRES EELIEEVGKD LRAMFSWLKD R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa.
[2]	"Purification of glutamyl-tRNA reductase from Synechocystis sp. PCC 6803." Rieble S., Beale S.I. J. Biol. Chem. 266:9740-9745(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-43.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA18666.1. Different initiation.
PIR	A47037. S76754.
RefSeq	NP_442854.1. NC_000911.1. YP_007452730.1. NC_020286.1.
3D structure databases
ProteinModelPortal	P29107.
SMR	P29107. Positions 3-328.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48805N.
IntAct	P29107. 1 interaction.
STRING	1148.sll1363.
Proteomic databases
PaxDb	P29107.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA18666; BAA18666; BAA18666.
GeneID	14618415. 952138.
KEGG	syn:sll1363.
PATRIC	23843490. VBISynSp132158_3280.
Phylogenomic databases
eggNOG	COG0059.
HOGENOM	HOG000016230.
KO	K00053.
OMA	MAYAKGI.
ProtClustDB	PRK05479.
Enzyme and pathway databases
UniPathway	UPA00047; UER00056. UPA00049; UER00060.
Family and domain databases
Gene3D	1.10.1040.10. 1 hit.
HAMAP	MF_00435. IlvC.
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR013023. AcH_isomrdctse. IPR000506. AcH_isomrdctse_C. IPR013328. DH_multihelical. IPR013116. IlvN. [Graphical view]
PANTHER	PTHR21371. PTHR21371. 1 hit.
Pfam	PF01450. IlvC. 1 hit. PF07991. IlvN. 1 hit. [Graphical view]
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMs	TIGR00465. ilvC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ILVC_SYNY3

Accession

Primary (citable) accession number: P29107
Secondary accession number(s): P74559

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program