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Q8RQN6 (ACEA_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. 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
Name:aceA
Ordered Locus Names:CE2232
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Cofactor

Divalent cations. Magnesium, manganese and cobalt can be used By similarity.

Pathway

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglyoxylate cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionisocitrate lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 431430Isocitrate lyase
PRO_0000068772

Sites

Active site1931 Probable

Experimental info

Sequence conflict4281G → C in BAB88666. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8RQN6 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: A6ACDA9530A6B207

FASTA43147,031
        10         20         30         40         50         60 
MSNVGTPRTA QEIQQDWDTN PRWNGITRDY TAEQVAELQG SVVEEHTLAK RGAEILWDAV 

        70         80         90        100        110        120 
SAEGDDYINA LGALTGNQAV QQVRAGLKAV YLSGWQVAGD ANLAGHTYPD QSLYPANSVP 

       130        140        150        160        170        180 
NVVRRINNAL LRADEIARVE GDTSVDNWLV PIVADGEAGF GGALNVYELQ KGMITAGAAG 

       190        200        210        220        230        240 
THWEDQLASE KKCGHLGGKV LIPTQQHIRT LNSARLAADV ANTPTVVIAR TDAEAATLIT 

       250        260        270        280        290        300 
SDVDERDRPF ITGERTAEGY YHVKPGLEPC IARAKSYAPY ADMIWMETGT PDLELAKKFA 

       310        320        330        340        350        360 
EGVRSEFPDQ LLSYNCSPSF NWSAHLEADE IAKFQKELGA MGFKFQFITL AGFHSLNYGM 

       370        380        390        400        410        420 
FDLAYGYARE GMPAFVDLQN REFKAAEERG FTAVKHQREV GAGYFDTIAT TVDPNSSTTA 

       430 
LKGSTEEGQF H 

« Hide

References

« Hide 'large scale' references
[1]"aceA of Corynebacterium efficiens."
Hirano S., Kimura E., Kawahara Y., Sugimoto S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.
[2]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB083050 Genomic DNA. Translation: BAB88666.1.
BA000035 Genomic DNA. Translation: BAC19042.1.
RefSeqNP_738842.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8RQN6.
SMRQ8RQN6. Positions 2-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196164.CE2232.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC19042; BAC19042; BAC19042.
GeneID1032083.
KEGGcef:CE2232.
PATRIC21490593. VBICorEff9312_2208.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000238475.
KOK01637.
OMAKEWWASP.
OrthoDBEOG689HMX.

Enzyme and pathway databases

UniPathwayUPA00703; UER00719.

Family and domain databases

Gene3D3.20.20.60. 1 hit.
InterProIPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamPF00463. ICL. 1 hit.
[Graphical view]
PIRSFPIRSF001362. Isocit_lyase. 1 hit.
SUPFAMSSF51621. SSF51621. 1 hit.
TIGRFAMsTIGR01346. isocit_lyase. 2 hits.
PROSITEPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACEA_COREF
AccessionPrimary (citable) accession number: Q8RQN6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 82 of the entry and version 4 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