P00894 (ILVH_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 110.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Acetolactate synthase isozyme 3 small subunit EC=2.2.1.6 Alternative name(s): ALS-III Acetohydroxy-acid synthase III small subunit Short name=AHAS-III | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 163 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | 2 pyruvate = 2-acetolactate + CO2. |
| Enzyme regulation | Sensitive to valine inhibition. |
| Pathway | Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4. |
| Subunit structure | Dimer of large and small chains. |
| Miscellaneous | E.coli contains genes for 3 AHAS isozymes: ilvBN, ilvGM and ilvIH. |
| Sequence similarities | Belongs to the acetolactate synthase small subunit family. Contains 1 ACT domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Branched-chain amino acid biosynthesis |
| Molecular function | Transferase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | isoleucine biosynthetic process Inferred from direct assay. Source: EcoCyc valine biosynthetic processInferred from direct assay. Source: EcoCyc |
| Molecular function | acetolactate synthase activity Inferred from direct assay. Source: EcoCyc amino acid bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 163 | 163 | Acetolactate synthase isozyme 3 small subunit | PRO_0000151410 | |||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||
| Domain | 3 – 76 | 74 | ACT | ||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 132 | 1 | D → S Ref.1 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 132 | 1 | D → S Ref.2 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 132 | 1 | D → S Ref.5 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 159 – 163 | 5 | DKIMR → VK in CAA25756. Ref.1 | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Beta strand | 2 – 10 | 9 | |||||||||||||||||||||||||||||||||||
| Helix | 15 – 24 | 10 | |||||||||||||||||||||||||||||||||||
| Turn | 25 – 27 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 31 – 37 | 7 | |||||||||||||||||||||||||||||||||||
| Beta strand | 41 – 52 | 12 | |||||||||||||||||||||||||||||||||||
| Helix | 54 – 66 | 13 | |||||||||||||||||||||||||||||||||||
| Beta strand | 70 – 75 | 6 | |||||||||||||||||||||||||||||||||||
| Helix | 76 – 78 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 81 – 92 | 12 | |||||||||||||||||||||||||||||||||||
| Helix | 96 – 107 | 12 | |||||||||||||||||||||||||||||||||||
| Beta strand | 111 – 115 | 5 | |||||||||||||||||||||||||||||||||||
| Beta strand | 117 – 126 | 10 | |||||||||||||||||||||||||||||||||||
| Helix | 128 – 138 | 11 | |||||||||||||||||||||||||||||||||||
| Turn | 139 – 141 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 142 – 149 | 8 | |||||||||||||||||||||||||||||||||||
| Beta strand | 153 – 157 | 5 | |||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular structure of ilvIH and its evolutionary relationship to ilvG in Escherichia coli K12." Squires C.H., Defelice M., Devereux J., Calvo J.M. Nucleic Acids Res. 11:5299-5313(1983) [PubMed: 6308579] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12. |
| [3] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 132. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "Nucleotide sequence of the ilvH-fruR gene region of Escherichia coli K12 and Salmonella typhimurium LT2." Jahreis K., Postma P.W., Lengeler J.W. Mol. Gen. Genet. 226:332-336(1991) [PubMed: 1851954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 130-163. Strain: K12. |
| [6] | "Molecular cloning, nucleotide sequence, and expression of shl, a new gene in the 2-minute region of the genetic map of Escherichia coli." Leclerc G., Noel G., Drapeau G.R. J. Bacteriol. 172:4696-4700(1990) [PubMed: 2198273] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 130-163. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X01609 Genomic DNA. Translation: CAA25756.1. X55457 Genomic DNA. No translation available. X55034 Genomic DNA. Translation: CAA38855.1. U00096 Genomic DNA. Translation: AAC73189.1. AP009048 Genomic DNA. Translation: BAB96647.2. M35034 Genomic DNA. Translation: AAA24627.1. | ||||||||||||
| PIR | YCEC3H. F64729. | ||||||||||||
| RefSeq | NP_414620.1. NC_000913.2. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P00894. | ||||||||||||
| SMR | P00894. Positions 2-163. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-10024N. | ||||||||||||
2D gel databases | |||||||||||||
| SWISS-2DPAGE | P00894. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | EBESCT00000002562; EBESCP00000002562; EBESCG00000002091. EBESCT00000002563; EBESCP00000002563; EBESCG00000002091. EBESCT00000002564; EBESCP00000002564; EBESCG00000002091. EBESCT00000002565; EBESCP00000002565; EBESCG00000002091. EBESCT00000015938; EBESCP00000015229; EBESCG00000014998. | ||||||||||||
| GeneID | 947267. | ||||||||||||
| GenomeReviews | Gene locus JW0077 in contig AP009048_GR. Gene locus b0078 in contig U00096_GR. | ||||||||||||
| KEGG | ecj:JW0077. eco:b0078. | ||||||||||||
| PATRIC | 32115259. VBIEscCol129921_0081. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB0494. | ||||||||||||
| EcoGene | EG10499. ilvH. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0440. | ||||||||||||
| GeneTree | EBGT00050000011172. | ||||||||||||
| HOGENOM | HBG335310. | ||||||||||||
| OMA | IERELAM. | ||||||||||||
| PhylomeDB | P00894. | ||||||||||||
| ProtClustDB | PRK11895. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:ACETOLACTSYNIII-HCHAIN-MONOMER. MetaCyc:ACETOLACTSYNIII-HCHAIN-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P00894. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR004789. Acetalactate_synth_ssu. IPR019455. Acetolactate_synth_ssu_C. IPR002912. ACT-bd. [Graphical view] | ||||||||||||
| KO | K01653. | ||||||||||||
| Pfam | PF01842. ACT. 1 hit. PF10369. ALS_ss_C. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR00119. Acolac_sm. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | ILVH_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P00894 Secondary accession number(s): P78046, Q47637 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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