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Protein

Isocitrate lyase

Gene

PA2634

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.By similarity

Catalytic activityi

Isocitrate = succinate + glyoxylate.By similarity

Cofactori

Mg2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi184 – 1841MagnesiumBy similarity
Active sitei222 – 2221Proton acceptorBy similarity
Binding sitei451 – 4511SubstrateBy similarity

GO - Molecular functioni

  1. isocitrate lyase activity Source: PseudoCAP

GO - Biological processi

  1. glyoxylate cycle Source: UniProtKB-UniPathway
  2. negative regulation of single-species biofilm formation on inanimate substrate Source: PseudoCAP
  3. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.1.3.1. 5087.
UniPathwayiUPA00703; UER00719.

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate lyaseBy similarity (EC:4.1.3.1By similarity)
Short name:
ICLBy similarity
Alternative name(s):
IsocitraseBy similarity
IsocitrataseBy similarity
Gene namesi
Ordered Locus Names:PA2634
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA2634.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 531531Isocitrate lyasePRO_0000068780Add
BLAST

Proteomic databases

PRIDEiQ9I0K4.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi208964.PA2634.

Structurei

3D structure databases

ProteinModelPortaliQ9I0K4.
SMRiQ9I0K4. Positions 79-506.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni101 – 1033Substrate bindingBy similarity
Regioni223 – 2242Substrate bindingBy similarity
Regioni380 – 3845Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2224.
HOGENOMiHOG000191811.
InParanoidiQ9I0K4.
KOiK01637.
OMAiFRWQVYD.
OrthoDBiEOG689HMX.
PhylomeDBiQ9I0K4.

Family and domain databases

Gene3Di3.20.20.60. 3 hits.
InterProiIPR006254. Isocitrate_lyase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamiPF00463. ICL. 3 hits.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9I0K4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAYQNEIKA VAALKEKNGS SWSAINPEYA ARMRIQNRFK TGLDIAKYTA
60 70 80 90 100
AIMRKDMAEY DADSSVYTQS LGCWHGFIGQ QKLISIKKHL KTTNKRYLYL
110 120 130 140 150
SGWMVAALRS DFGPLPDQSM HEKTAVSGLI EELYTFLRQA DARELDLLFT
160 170 180 190 200
GLDAARAAGD KAKEAELLAQ IDNFETHVVP IIADIDAGFG NAEATYLLAK
210 220 230 240 250
KMIEAGACCI QIENQVSDEK QCGHQDGKVT VPHIDFLAKI NAVRYAFLEL
260 270 280 290 300
GVDDGVIVAR TDSLGAGLTK QIAVTNEPGD LGDLYNSFLD CEEISESELG
310 320 330 340 350
NGDVVIKREG KLLRPKRLAS NLFQFRKGTG EDRCVLDCIT SLQNGADLLW
360 370 380 390 400
IETEKPHVGQ IKAMVDRIRE VIPNAKLVYN NSPSFNWTLN FRQQVFDAFV
410 420 430 440 450
AEGKDVSAYD RNKLMSVEYD DTELAKVADE KIRTFQRDGS AHAGIFHHLI
460 470 480 490 500
TLPTYHTAAL STDNLAKGYF ADEGMLAYVK GVQRQELRQG IACVKHQNMA
510 520 530
GSDIGDNHKE YFAGEAALKA SGKDNTMNQF H
Length:531
Mass (Da):58,887
Last modified:February 28, 2001 - v1
Checksum:iF45A4ECDA3F220CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG06022.1.
PIRiG83315.
RefSeqiNP_251324.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG06022; AAG06022; PA2634.
GeneIDi882341.
KEGGipae:PA2634.
PATRICi19839761. VBIPseAer58763_2756.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG06022.1.
PIRiG83315.
RefSeqiNP_251324.1. NC_002516.2.

3D structure databases

ProteinModelPortaliQ9I0K4.
SMRiQ9I0K4. Positions 79-506.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA2634.

Proteomic databases

PRIDEiQ9I0K4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG06022; AAG06022; PA2634.
GeneIDi882341.
KEGGipae:PA2634.
PATRICi19839761. VBIPseAer58763_2756.

Organism-specific databases

PseudoCAPiPA2634.

Phylogenomic databases

eggNOGiCOG2224.
HOGENOMiHOG000191811.
InParanoidiQ9I0K4.
KOiK01637.
OMAiFRWQVYD.
OrthoDBiEOG689HMX.
PhylomeDBiQ9I0K4.

Enzyme and pathway databases

UniPathwayiUPA00703; UER00719.
BRENDAi4.1.3.1. 5087.

Family and domain databases

Gene3Di3.20.20.60. 3 hits.
InterProiIPR006254. Isocitrate_lyase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamiPF00463. ICL. 3 hits.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. "Biofouling in water treatment systems: effect of membrane properties on biofilm formation."
    Liddor M.
    Thesis (2004), Ben-Gurion University, Israel
    Cited for: PROTEIN SEQUENCE OF 110-138; 144-156; 245-260; 318-325; 393-404; 414-426 AND 468-480.
    Strain: ATCC 33467 / type 1 smooth.

Entry informationi

Entry nameiACEA_PSEAE
AccessioniPrimary (citable) accession number: Q9I0K4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2005
Last sequence update: February 28, 2001
Last modified: March 31, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.