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Protein

Acetolactate synthase, catabolic

Gene

budB

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 pyruvate = 2-acetolactate + CO2.

pH dependencei

Optimum pH is 6.

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, catabolic (budB)
  2. no protein annotated in this organism
  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 sitei159 – 1591FADBy similarity
Metal bindingi447 – 4471MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi263 – 28422FADBy similarityAdd
BLAST
Nucleotide bindingi304 – 32320FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15237.
UniPathwayiUPA00626; UER00677.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetolactate synthase, catabolic (EC:2.2.1.6)
Short name:
ALS
Gene namesi
Name:budB
Synonyms:ilvK
OrganismiKlebsiella pneumoniae
Taxonomic identifieri573 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Acetolactate synthase, catabolicPRO_0000090797Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272620.KPN_02060.

Structurei

Secondary structure

1
559
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114Combined sources
Helixi13 – 2311Combined sources
Beta strandi28 – 325Combined sources
Turni35 – 373Combined sources
Helixi38 – 436Combined sources
Helixi44 – 463Combined sources
Beta strandi47 – 537Combined sources
Helixi57 – 7115Combined sources
Beta strandi75 – 795Combined sources
Helixi83 – 864Combined sources
Helixi89 – 9810Combined sources
Beta strandi102 – 1087Combined sources
Turni111 – 1133Combined sources
Turni114 – 1196Combined sources
Helixi124 – 1285Combined sources
Helixi129 – 1313Combined sources
Beta strandi133 – 1375Combined sources
Helixi141 – 1433Combined sources
Helixi144 – 15613Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi162 – 1687Combined sources
Helixi169 – 1735Combined sources
Beta strandi176 – 1783Combined sources
Helixi194 – 20613Combined sources
Beta strandi208 – 2147Combined sources
Helixi216 – 2194Combined sources
Helixi221 – 2233Combined sources
Helixi224 – 23411Combined sources
Beta strandi238 – 2403Combined sources
Helixi242 – 2443Combined sources
Turni245 – 2473Combined sources
Turni250 – 2523Combined sources
Beta strandi256 – 2594Combined sources
Beta strandi261 – 2633Combined sources
Helixi267 – 2748Combined sources
Beta strandi276 – 2827Combined sources
Helixi285 – 2873Combined sources
Helixi290 – 2923Combined sources
Beta strandi298 – 3069Combined sources
Beta strandi317 – 3226Combined sources
Helixi324 – 33310Combined sources
Helixi343 – 36018Combined sources
Beta strandi369 – 3713Combined sources
Helixi373 – 38311Combined sources
Beta strandi388 – 3925Combined sources
Helixi396 – 4038Combined sources
Helixi404 – 4074Combined sources
Beta strandi411 – 4144Combined sources
Helixi425 – 43511Combined sources
Beta strandi439 – 4468Combined sources
Helixi447 – 4537Combined sources
Helixi456 – 4638Combined sources
Beta strandi467 – 4737Combined sources
Helixi478 – 48811Combined sources
Helixi501 – 5066Combined sources
Turni507 – 5093Combined sources
Beta strandi510 – 5145Combined sources
Helixi518 – 5203Combined sources
Helixi521 – 53010Combined sources
Beta strandi531 – 5333Combined sources
Beta strandi535 – 5417Combined sources
Helixi543 – 5453Combined sources
Helixi546 – 5505Combined sources
Helixi554 – 5563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OZFX-ray2.30A/B1-559[»]
1OZGX-ray2.30A/B1-559[»]
1OZHX-ray2.00A/B/C/D1-559[»]
ProteinModelPortaliP27696.
SMRiP27696. Positions 6-554.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27696.

Family & Domainsi

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105C7K. Bacteria.
COG0028. LUCA.

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.

P27696-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKQYPVRQW AHGADLVVSQ LEAQGVRQVF GIPGAKIDKV FDSLLDSSIR
60 70 80 90 100
IIPVRHEANA AFMAAAVGRI TGKAGVALVT SGPGCSNLIT GMATANSEGD
110 120 130 140 150
PVVALGGAVK RADKAKQVHQ SMDTVAMFSP VTKYAIEVTA PDALAEVVSN
160 170 180 190 200
AFRAAEQGRP GSAFVSLPQD VVDGPVSGKV LPASGAPQMG AAPDDAIDQV
210 220 230 240 250
AKLIAQAKNP IFLLGLMASQ PENSKALRRL LETSHIPVTS TYQAAGAVNQ
260 270 280 290 300
DNFSRFAGRV GLFNNQAGDR LLQLADLVIC IGYSPVEYEP AMWNSGNATL
310 320 330 340 350
VHIDVLPAYE ERNYTPDVEL VGDIAGTLNK LAQNIDHRLV LSPQAAEILR
360 370 380 390 400
DRQHQRELLD RRGAQLNQFA LHPLRIVRAM QDIVNSDVTL TVDMGSFHIW
410 420 430 440 450
IARYLYTFRA RQVMISNGQQ TMGVALPWAI GAWLVNPERK VVSVSGDGGF
460 470 480 490 500
LQSSMELETA VRLKANVLHL IWVDNGYNMV AIQEEKKYQR LSGVEFGPMD
510 520 530 540 550
FKAYAESFGA KGFAVESAEA LEPTLRAAMD VDGPAVVAIP VDYRDNPLLM

GQLHLSQIL
Length:559
Mass (Da):60,338
Last modified:August 1, 1992 - v1
Checksum:i7775373ABEEE603D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73842 Genomic DNA. Translation: AAA25079.1.
PIRiJC1218.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73842 Genomic DNA. Translation: AAA25079.1.
PIRiJC1218.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OZFX-ray2.30A/B1-559[»]
1OZGX-ray2.30A/B1-559[»]
1OZHX-ray2.00A/B/C/D1-559[»]
ProteinModelPortaliP27696.
SMRiP27696. Positions 6-554.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272620.KPN_02060.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C7K. Bacteria.
COG0028. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00626; UER00677.
BioCyciMetaCyc:MONOMER-15237.

Miscellaneous databases

EvolutionaryTraceiP27696.

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...

Publicationsi

  1. "Cloning, sequencing and heterologous expression of a Klebsiella pneumoniae gene encoding an FAD-independent acetolactate synthase."
    Peng H.-L., Wang P.-Y., Wu C.-M., Hwang D.-C., Chang H.-Y.
    Gene 117:125-130(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate."
    Pang S.S., Duggleby R.G., Schowen R.L., Guddat L.W.
    J. Biol. Chem. 279:2242-2253(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiILVB_KLEPN
AccessioniPrimary (citable) accession number: P27696
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 11, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Does not seem to require thiamine pyrophosphate.
Valine resistant.

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.