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Q9I0K4 (ACEA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate lyase

Short name=ICL
Short name=Isocitrase
Short name=Isocitratase
EC=4.1.3.1
Gene names
Ordered Locus Names:PA2634
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle. May be involved in the assimilation of one-carbon compounds via the isocitrate lyase-positive serine pathway By similarity.

Catalytic activity

Isocitrate = succinate + glyoxylate. UniProtKB P28298

Pathway

Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 1/2.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 531531Isocitrate lyase
PRO_0000068780

Sites

Active site2221 By similarity UniProtKB P28298

Sequences

Sequence LengthMass (Da)Tools
Q9I0K4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F45A4ECDA3F220CA

FASTA53158,887
        10         20         30         40         50         60 
MSAYQNEIKA VAALKEKNGS SWSAINPEYA ARMRIQNRFK TGLDIAKYTA AIMRKDMAEY 

        70         80         90        100        110        120 
DADSSVYTQS LGCWHGFIGQ QKLISIKKHL KTTNKRYLYL SGWMVAALRS DFGPLPDQSM 

       130        140        150        160        170        180 
HEKTAVSGLI EELYTFLRQA DARELDLLFT GLDAARAAGD KAKEAELLAQ IDNFETHVVP 

       190        200        210        220        230        240 
IIADIDAGFG NAEATYLLAK KMIEAGACCI QIENQVSDEK QCGHQDGKVT VPHIDFLAKI 

       250        260        270        280        290        300 
NAVRYAFLEL GVDDGVIVAR TDSLGAGLTK QIAVTNEPGD LGDLYNSFLD CEEISESELG 

       310        320        330        340        350        360 
NGDVVIKREG KLLRPKRLAS NLFQFRKGTG EDRCVLDCIT SLQNGADLLW IETEKPHVGQ 

       370        380        390        400        410        420 
IKAMVDRIRE VIPNAKLVYN NSPSFNWTLN FRQQVFDAFV AEGKDVSAYD RNKLMSVEYD 

       430        440        450        460        470        480 
DTELAKVADE KIRTFQRDGS AHAGIFHHLI TLPTYHTAAL STDNLAKGYF ADEGMLAYVK 

       490        500        510        520        530 
GVQRQELRQG IACVKHQNMA GSDIGDNHKE YFAGEAALKA SGKDNTMNQF H 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
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 (2005), 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG06022.1.
PIRG83315.
RefSeqNP_251324.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9I0K4.
SMRQ9I0K4. Positions 16-514.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA2634.

Proteomic databases

PRIDEQ9I0K4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID882341.
KEGGpae:PA2634.
PATRIC19839761. VBIPseAer58763_2756.

Organism-specific databases

PseudoCAPPA2634.

Phylogenomic databases

eggNOGCOG2224.
HOGENOMHOG000191811.
KOK01637.
OMAFRWQVYD.
OrthoDBEOG689HMX.
ProtClustDBPRK06498.

Enzyme and pathway databases

BRENDA4.1.3.1. 5087.
UniPathwayUPA00703; UER00719.

Family and domain databases

Gene3D3.20.20.60. 3 hits.
InterProIPR006254. Isocitrate_lyase.
IPR000918. Isocitrate_lyase/Pmutase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamPF00463. ICL. 3 hits.
[Graphical view]
PIRSFPIRSF001362. Isocit_lyase. 1 hit.
SUPFAMSSF51621. SSF51621. 2 hits.
ProtoNetSearch...

Entry information

Entry nameACEA_PSEAE
AccessionPrimary (citable) accession number: Q9I0K4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways