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P29107 (ILVC_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 331330Ketol-acid reductoisomerase HAMAP-Rule MF_00435
PRO_0000151372

Sites

Active site1081 Potential

Sequences

Sequence LengthMass (Da)Tools
P29107 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 070C9D494F39CD44

FASTA33135,822
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
PIRA47037. S76754.
RefSeqNP_442854.1. NC_000911.1.
YP_007452730.1. NC_020286.1.

3D structure databases

ProteinModelPortalP29107.
SMRP29107. Positions 3-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48805N.
IntActP29107. 1 interaction.
STRING1148.sll1363.

Proteomic databases

PaxDbP29107.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA18666; BAA18666; BAA18666.
GeneID14618415.
952138.
KEGGsyn:sll1363.
syz:MYO_129910.
PATRIC23843490. VBISynSp132158_3280.

Phylogenomic databases

eggNOGCOG0059.
HOGENOMHOG000016230.
KOK00053.
OMAEWILENQ.
OrthoDBEOG625K07.
PhylomeDBP29107.
ProtClustDBPRK05479.

Enzyme and pathway databases

UniPathwayUPA00047; UER00056.
UPA00049; UER00060.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
HAMAPMF_00435. IlvC.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR013023. AcH_isomrdctse.
IPR000506. AcH_isomrdctse_C.
IPR013328. DH_multihelical.
IPR013116. IlvN.
[Graphical view]
PANTHERPTHR21371. PTHR21371. 1 hit.
PfamPF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 1 hit.
TIGRFAMsTIGR00465. ilvC. 1 hit.
ProtoNetSearch...

Entry information

Entry nameILVC_SYNY3
AccessionPrimary (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: April 16, 2014
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways