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Protein

Acetolactate synthase

Gene

alsS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

2 pyruvate = 2-acetolactate + CO2.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity
  • thiamine diphosphateBy similarityNote: Binds 1 thiamine pyrophosphate per subunit.By similarity

Pathwayi: (R,R)-butane-2,3-diol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R,R)-butane-2,3-diol from pyruvate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Acetolactate synthase (alsS)
  2. Alpha-acetolactate decarboxylase (alsD)
  3. no protein annotated in this organism
This subpathway is part of the pathway (R,R)-butane-2,3-diol biosynthesis, which is itself part of Polyol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R,R)-butane-2,3-diol from pyruvate, the pathway (R,R)-butane-2,3-diol biosynthesis and in Polyol metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Thiamine pyrophosphateBy similarity
Binding sitei162 – 1621FADBy similarity
Metal bindingi450 – 4501MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi266 – 28722FADBy similarityAdd
BLAST
Nucleotide bindingi308 – 32720FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Acetoin biosynthesis

Keywords - Ligandi

FAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciBSUB:BSU36010-MONOMER.
UniPathwayiUPA00626; UER00677.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetolactate synthase (EC:2.2.1.6)
Alternative name(s):
ALS
Acetohydroxy-acid synthase
Gene namesi
Name:alsS
Ordered Locus Names:BSU36010
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 570570Acetolactate synthasePRO_0000090799Add
BLAST

Proteomic databases

PaxDbiQ04789.

Expressioni

Inductioni

Strongly induced under anaerobic conditions. Activated by ResDE, Fnr and ArfM.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019476.

Structurei

3D structure databases

ProteinModelPortaliQ04789.
SMRiQ04789. Positions 13-553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni399 – 47981Thiamine pyrophosphate bindingAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiCOG0028. LUCA.
HOGENOMiHOG000258447.
InParanoidiQ04789.
KOiK01652.
OMAiNGYNMVA.
PhylomeDBiQ04789.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR012782. Acetolactate_synth_catblc.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR02418. acolac_catab. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04789-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKATKEQKS LVKNRGAELV VDCLVEQGVT HVFGIPGAKI DAVFDALQDK
60 70 80 90 100
GPEIIVARHE QNAAFMAQAV GRLTGKPGVV LVTSGPGASN LATGLLTANT
110 120 130 140 150
EGDPVVALAG NVIRADRLKR THQSLDNAAL FQPITKYSVE VQDVKNIPEA
160 170 180 190 200
VTNAFRIASA GQAGAAFVSF PQDVVNEVTN TKNVRAVAAP KLGPAADDAI
210 220 230 240 250
SAAIAKIQTA KLPVVLVGMK GGRPEAIKAV RKLLKKVQLP FVETYQAAGT
260 270 280 290 300
LSRDLEDQYF GRIGLFRNQP GDLLLEQADV VLTIGYDPIE YDPKFWNING
310 320 330 340 350
DRTIIHLDEI IADIDHAYQP DLELIGDIPS TINHIEHDAV KVEFAEREQK
360 370 380 390 400
ILSDLKQYMH EGEQVPADWK SDRAHPLEIV KELRNAVDDH VTVTCDIGSH
410 420 430 440 450
AIWMSRYFRS YEPLTLMISN GMQTLGVALP WAIGASLVKP GEKVVSVSGD
460 470 480 490 500
GGFLFSAMEL ETAVRLKAPI VHIVWNDSTY DMVAFQQLKK YNRTSAVDFG
510 520 530 540 550
NIDIVKYAES FGATGLRVES PDQLADVLRQ GMNAEGPVII DVPVDYSDNI
560 570
NLASDKLPKE FGELMKTKAL
Length:570
Mass (Da):62,004
Last modified:June 16, 2009 - v3
Checksum:i47B7A64CE6C78EF7
GO

Sequence cautioni

The sequence AAA22222 differs from that shown. Reason: Frameshift at position 64. Curated
The sequence CAB07802 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161D → Y in AAA22222 (PubMed:7685336).Curated
Sequence conflicti401 – 4011A → S in AAA22222 (PubMed:7685336).Curated
Sequence conflicti484 – 4841A → H in AAA22222 (PubMed:7685336).Curated
Sequence conflicti515 – 5151G → A in AAA22222 (PubMed:7685336).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04470 Genomic DNA. Translation: AAA22222.1. Frameshift.
Z93767 Genomic DNA. Translation: CAB07802.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB15618.2.
PIRiH69584.
RefSeqiNP_391482.2. NC_000964.3.
WP_003244057.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15618; CAB15618; BSU36010.
GeneIDi936852.
KEGGibsu:BSU36010.
PATRICi18979222. VBIBacSub10457_3773.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04470 Genomic DNA. Translation: AAA22222.1. Frameshift.
Z93767 Genomic DNA. Translation: CAB07802.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB15618.2.
PIRiH69584.
RefSeqiNP_391482.2. NC_000964.3.
WP_003244057.1. NZ_JNCM01000034.1.

3D structure databases

ProteinModelPortaliQ04789.
SMRiQ04789. Positions 13-553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019476.

Proteomic databases

PaxDbiQ04789.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15618; CAB15618; BSU36010.
GeneIDi936852.
KEGGibsu:BSU36010.
PATRICi18979222. VBIBacSub10457_3773.

Phylogenomic databases

eggNOGiCOG0028. LUCA.
HOGENOMiHOG000258447.
InParanoidiQ04789.
KOiK01652.
OMAiNGYNMVA.
PhylomeDBiQ04789.

Enzyme and pathway databases

UniPathwayiUPA00626; UER00677.
BioCyciBSUB:BSU36010-MONOMER.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR012782. Acetolactate_synth_catblc.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR02418. acolac_catab. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiILVX_BACSU
AccessioniPrimary (citable) accession number: Q04789
Secondary accession number(s): O05225
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 16, 2009
Last modified: September 7, 2016
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.