Acetolactate synthase isozyme 3 large subunit - Escherichia coli (strain K12)

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P00893 (ILVI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acetolactate synthase isozyme 3 large subunit
EC=2.2.1.6

Alternative name(s):
AHAS-III
ALS-III
Acetohydroxy-acid synthase III large subunit

Gene names

Name:	ilvI
Ordered Locus Names:	b0077, JW0076

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	574 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	2 pyruvate = 2-acetolactate + CO₂.
Cofactor	Binds 1 magnesium ion per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity.
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. Contains 1 molecule of FAD per monomer. The role of this cofactor is not clear considering that the reaction does not involve redox chemistry By similarity.
Sequence similarities	Belongs to the TPP enzyme family.
Sequence caution	The sequence CAA25755.1 differs from that shown. Reason: Frameshift at position 523.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Ligand	FAD Flavoprotein Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	isoleucine biosynthetic process Inferred from direct assay PubMed 2675968. Source: EcoCyc valine biosynthetic process Inferred from direct assay PubMed 2675968. Source: EcoCyc
Molecular_function	acetolactate synthase activity Inferred from direct assay PubMed 2675968. Source: EcoCyc flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro thiamine pyrophosphate binding Inferred 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 – 574

574

Acetolactate synthase isozyme 3 large subunit

PRO_0000090789

Regions

Nucleotide binding

261 – 282

FAD By similarity

Nucleotide binding

304 – 323

FAD By similarity

Region

397 – 477

Thiamine pyrophosphate binding

Sites

Metal binding

448

Magnesium By similarity

Metal binding

475

Magnesium By similarity

Binding site

Thiamine pyrophosphate By similarity

Binding site

153

FAD By similarity

Experimental info

Sequence conflict

202 – 203

TL → SV in CAA25755. Ref.1

Sequence conflict

202 – 203

TL → SV in CAA38854. Ref.5

Sequence conflict

206

A → V in CAA25755. Ref.1

Sequence conflict

206

A → V in CAA38854. Ref.5

Sequence conflict

254

A → V in CAA25755. Ref.1

Sequence conflict

254

A → V in CAA38854. Ref.5

Sequence conflict

422

T → S in CAA25755. Ref.1

Sequence conflict

422

T → S in CAA38854. Ref.5

Sequence conflict

437 – 438

LP → FA in CAA38854. Ref.5

Sequence conflict

507 – 509

LAE → RG in CAA25755. Ref.1

Sequence conflict

507 – 509

LAE → RG in CAA38854. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P00893 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: B62DEF64338CBF8C
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FASTA

574

62,984

        10         20         30         40         50         60 
MEMLSGAEMV VRSLIDQGVK QVFGYPGGAV LDIYDALHTV GGIDHVLVRH EQAAVHMADG 

        70         80         90        100        110        120 
LARATGEVGV VLVTSGPGAT NAITGIATAY MDSIPLVVLS GQVATSLIGY DAFQECDMVG 

       130        140        150        160        170        180 
ISRPVVKHSF LVKQTEDIPQ VLKKAFWLAA SGRPGPVVVD LPKDILNPAN KLPYVWPESV 

       190        200        210        220        230        240 
SMRSYNPTTT GHKGQIKRAL QTLVAAKKPV VYVGGGAITA GCHQQLKETV EALNLPVVCS 

       250        260        270        280        290        300 
LMGLGAFPAT HRQALGMLGM HGTYEANMTM HNADVIFAVG VRFDDRTTNN LAKYCPNATV 

       310        320        330        340        350        360 
LHIDIDPTSI SKTVTADIPI VGDARQVLEQ MLELLSQESA HQPLDEIRDW WQQIEQWRAR 

       370        380        390        400        410        420 
QCLKYDTHSE KIKPQAVIET LWRLTKGDAY VTSDVGQHQM FAALYYPFDK PRRWINSGGL 

       430        440        450        460        470        480 
GTMGFGLPAA LGVKMALPEE TVVCVTGDGS IQMNIQELST ALQYELPVLV VNLNNRYLGM 

       490        500        510        520        530        540 
VKQWQDMIYS GRHSQSYMQS LPDFVRLAEA YGHVGIQISH PHELESKLSE ALEQVRNNRL 

       550        560        570 
VFVDVTVDGS EHVYPMQIRG GGMDEMWLSK TERT

« Hide

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Regulation of transcription at the 2-minute region of the genetic map of Escherichia coli." Ayala J.A. Submitted (JAN-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Unusual organization of the ilvIH promoter of Escherichia coli." Haughn G.W., Squires C.H., Defelice M., Largo C.T., Calvo J.M. J. Bacteriol. 163:186-198(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X01609 Genomic DNA. Translation: CAA25755.1. Frameshift. U00096 Genomic DNA. Translation: AAC73188.2. AP009048 Genomic DNA. Translation: BAB96646.2. X55034 Genomic DNA. Translation: CAA38854.1. M10738 Genomic DNA. Translation: AAA24026.1.
PIR	YCEC3I. E64729.
RefSeq	YP_025294.2. NC_000913.2. YP_488383.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P00893.
SMR	P00893. Positions 4-565.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6850N.
IntAct	P00893. 3 interactions.
STRING	511145.b0077.
Proteomic databases
PaxDb	P00893.
PRIDE	P00893.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73188; AAC73188; b0077. BAB96646; BAB96646; BAB96646.
GeneID	12930386. 948793.
KEGG	ecj:Y75_p0077. eco:b0077.
PATRIC	32115257. VBIEscCol129921_0080.
Organism-specific databases
EchoBASE	EB0495.
EcoGene	EG10500. ilvI.
Phylogenomic databases
eggNOG	COG0028.
HOGENOM	HOG000258448.
KO	K01652.
OMA	MAMQNCD.
ProtClustDB	PRK07979.
Enzyme and pathway databases
BioCyc	EcoCyc:ACETOLACTSYNIII-ICHAIN-MONOMER. ECOL316407:JW0076-MONOMER. MetaCyc:ACETOLACTSYNIII-ICHAIN-MONOMER.
UniPathway	UPA00047; UER00055. UPA00049; UER00059.
Gene expression databases
Genevestigator	P00893.
Family and domain databases
InterPro	IPR012846. Acetolactate_synth_lsu. IPR012000. Thiamin_PyroP_enz_cen_dom. IPR012001. Thiamin_PyroP_enz_TPP-bd_dom. IPR000399. TPP-bd_CS. IPR011766. TPP_enzyme-bd_C. [Graphical view]
PANTHER	PTHR18968:SF13. PTHR18968:SF13. 1 hit.
Pfam	PF02775. TPP_enzyme_C. 1 hit. PF00205. TPP_enzyme_M. 1 hit. PF02776. TPP_enzyme_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00118. acolac_lg. 1 hit.
PROSITE	PS00187. TPP_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ILVI_ECOLI

Accession

Primary (citable) accession number: P00893
Secondary accession number(s): P78045

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete 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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents