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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)DescriptionActionsGraphical viewLength
Binding sitei159FADBy similarity1
Metal bindingi447MagnesiumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi263 – 284FADBy similarityAdd BLAST22
Nucleotide bindingi304 – 323FADBy similarityAdd BLAST20

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeKlebsiella

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000907971 – 559Acetolactate synthase, catabolicAdd BLAST559

Interactioni

Protein-protein interaction databases

STRINGi272620.KPN_02060.

Structurei

Secondary structure

1559
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi8 – 11Combined sources4
Helixi13 – 23Combined sources11
Beta strandi28 – 32Combined sources5
Turni35 – 37Combined sources3
Helixi38 – 43Combined sources6
Helixi44 – 46Combined sources3
Beta strandi47 – 53Combined sources7
Helixi57 – 71Combined sources15
Beta strandi75 – 79Combined sources5
Helixi83 – 86Combined sources4
Helixi89 – 98Combined sources10
Beta strandi102 – 108Combined sources7
Turni111 – 113Combined sources3
Turni114 – 117Combined sources4
Helixi124 – 128Combined sources5
Helixi129 – 131Combined sources3
Beta strandi133 – 137Combined sources5
Helixi141 – 143Combined sources3
Helixi144 – 156Combined sources13
Beta strandi157 – 159Combined sources3
Beta strandi162 – 168Combined sources7
Helixi169 – 173Combined sources5
Beta strandi176 – 178Combined sources3
Helixi194 – 206Combined sources13
Beta strandi208 – 214Combined sources7
Helixi216 – 219Combined sources4
Helixi221 – 223Combined sources3
Helixi224 – 234Combined sources11
Beta strandi238 – 240Combined sources3
Helixi242 – 244Combined sources3
Turni245 – 247Combined sources3
Turni250 – 252Combined sources3
Beta strandi256 – 259Combined sources4
Beta strandi261 – 263Combined sources3
Helixi267 – 274Combined sources8
Beta strandi276 – 282Combined sources7
Helixi285 – 287Combined sources3
Helixi290 – 292Combined sources3
Beta strandi298 – 306Combined sources9
Beta strandi317 – 322Combined sources6
Helixi324 – 333Combined sources10
Helixi343 – 360Combined sources18
Beta strandi369 – 371Combined sources3
Helixi373 – 383Combined sources11
Beta strandi388 – 392Combined sources5
Helixi396 – 403Combined sources8
Helixi404 – 407Combined sources4
Beta strandi411 – 414Combined sources4
Helixi425 – 435Combined sources11
Beta strandi439 – 446Combined sources8
Helixi447 – 453Combined sources7
Helixi456 – 463Combined sources8
Beta strandi467 – 473Combined sources7
Helixi478 – 488Combined sources11
Helixi501 – 506Combined sources6
Turni507 – 509Combined sources3
Beta strandi510 – 514Combined sources5
Helixi518 – 520Combined sources3
Helixi521 – 530Combined sources10
Beta strandi531 – 533Combined sources3
Beta strandi535 – 541Combined sources7
Helixi543 – 545Combined sources3
Helixi546 – 550Combined sources5
Helixi554 – 556Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OZFX-ray2.30A/B1-559[»]
1OZGX-ray2.30A/B1-559[»]
1OZHX-ray2.00A/B/C/D1-559[»]
5D6RX-ray2.28B/M1-559[»]
5DX6X-ray1.75A/B1-559[»]
ProteinModelPortaliP27696.
SMRiP27696.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OZFX-ray2.30A/B1-559[»]
1OZGX-ray2.30A/B1-559[»]
1OZHX-ray2.00A/B/C/D1-559[»]
5D6RX-ray2.28B/M1-559[»]
5DX6X-ray1.75A/B1-559[»]
ProteinModelPortaliP27696.
SMRiP27696.
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...

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 30, 2016
This is version 91 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.