Acetolactate synthase large subunit - Lactococcus lactis subsp. lactis (strain IL1403)

Contribute

Send feedback

Read comments (?) or add your own

Q02137 (ILVB_LACLA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 95. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

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 large subunit
Short name=AHAS
EC=2.2.1.6

Alternative name(s):
Acetohydroxy-acid synthase large subunit
Short name=ALS

Gene names

Name:	ilvB
Ordered Locus Names:	LL1224
ORF Names:	L0078

Organism

Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)

Taxonomic identifier

272623 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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.
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	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 AAK05322.1 differs from that shown. Reason: Erroneous termination at position 5. Translated as Lys.

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 Reference proteome
Gene Ontology (GO)
Biological process	branched chain family amino acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	acetolactate synthase activity Inferred from electronic annotation. Source: EC 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 – 575

575

Acetolactate synthase large subunit

PRO_0000090785

Regions

Nucleotide binding

265 – 286

FAD By similarity

Nucleotide binding

308 – 327

FAD By similarity

Region

395 – 475

Thiamine pyrophosphate binding

Sites

Metal binding

446

Magnesium By similarity

Metal binding

473

Magnesium By similarity

Binding site

Thiamine pyrophosphate By similarity

Binding site

159

FAD By similarity

Experimental info

Sequence conflict

111 – 112

PL → RQ in AAB81919. Ref.1

Sequence conflict

298

V → F in AAB81919. Ref.1

Sequence conflict

353 – 354

TK → IE in AAB81919. Ref.1

Sequence conflict

557

S → N in AAB81919. Ref.1

Sequence conflict

568

E → K in AAB81919. Ref.1

Sequence conflict

572

V → I in AAB81919. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q02137 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 2F7168C50409035F
Show »

FASTA

575

62,850

        10         20         30         40         50         60 
MKKIKLEKPT SGSQLVLQTL KELGVEIIFG YPGGAMLPLY DAIHNFEGIQ HILARHEQGA 

        70         80         90        100        110        120 
THEAEGYAKS SGKVGVVVVT SGPGATNAVT GIADAYLDSV PLLVFTGQVG PLSIGKDAFQ 

       130        140        150        160        170        180 
EADTVGITAP ITKYNYQIRE TADIPRIVTE AYYLARTGRP GPVEIDLPKD VSTLEVTEIN 

       190        200        210        220        230        240 
DPSLNLPHYH ESEKATDEQL QELLTELSVS KKPVIIAGGG INYSGSVDIF RAFVEKYQIP 

       250        260        270        280        290        300 
VVSTLLGLGT LPISHELQLG MAGMHGSYAA NMALVEADYI INLGSRFDDR VVSNPAKVAK 

       310        320        330        340        350        360 
NAVVAHIDID AAELGKIVKT DIPILSDLKA ALSRLLQLNK VRTDFNDWIK TVTKNKEKAP 

       370        380        390        400        410        420 
FTYEPQNHDI RPQETIKLIG EYTQGDAIIV TDVGQHQMWV AQYYPYKNAR QLITSGGMGT 

       430        440        450        460        470        480 
MGFGIPAAIG AKLAQPNKNV IVFVGDGGFQ MTNQELALLN GYGIAIKVVL INNHSLGMVR 

       490        500        510        520        530        540 
QWQESFYEER RSQSVFDVEP NFQLLAEAYG IKHVKLDNPK TLADDLKIIT EDEPMLIEVL 

       550        560        570 
ISKSEHVLPM IPAGLHSDEM IGLHFTDENE EVDNA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp. lactis." Godon J.-J., Chopin M.-C., Ehrlich S.D. J. Bacteriol. 174:6580-6589(1992) [PubMed: 1400210] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCDO 2118.
[2]	"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403." Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A. Genome Res. 11:731-753(2001) [PubMed: 11337471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IL1403.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U92974 Genomic DNA. Translation: AAB81919.1. AE005176 Genomic DNA. Translation: AAK05322.1. Sequence problems.
PIR	H86777. S35138.
RefSeq	NP_267380.1. NC_002662.1.
3D structure databases
ProteinModelPortal	Q02137.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1114873.
GenomeReviews	Gene locus LL1224 in contig AE005176_GR.
KEGG	lla:L0078.
NMPDR	fig\|272623.1.peg.1259.
PATRIC	22294830. VBILacLac136773_1323.
Phylogenomic databases
HOGENOM	HBG323037.
ProtClustDB	PRK07282.
Enzyme and pathway databases
BioCyc	LLAC272623:L0078-MONOMER.
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]
KO	K01652.
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

ILVB_LACLA

Accession

Primary (citable) accession number: Q02137
Secondary accession number(s): Q9CG84

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	September 26, 2001
Last modified:	January 25, 2012
This is version 95 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

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

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents