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P9WKK7 (ACEA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 4. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:icl
Ordered Locus Names:Rv0467
ORF Names:MTV038.11
OrganismMycobacterium tuberculosis (strain ATCC 25618 / H37Rv) [Reference proteome] [HAMAP]
Taxonomic identifier83332 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length428 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.

Pathway

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm.

Post-translational modification

Pupylated at Lys-334 by the prokaryotic ubiquitin-like protein Pup, which leads to its degradation by the proteasome. Ref.2

Miscellaneous

Was identified as a natural substrate of the M.tuberculosis proteasome.

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
   PTMIsopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference 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

Chain1 – 428428Isocitrate lyase
PRO_0000068779

Sites

Active site1911

Amino acid modifications

Cross-link334Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Secondary structure

......................................................................... 428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P9WKK7 [UniParc].

Last modified April 16, 2014. Version 1.
Checksum: E5223F38CB5D9E8B

FASTA42847,087
        10         20         30         40         50         60 
MSVVGTPKSA EQIQQEWDTN PRWKDVTRTY SAEDVVALQG SVVEEHTLAR RGAEVLWEQL 

        70         80         90        100        110        120 
HDLEWVNALG ALTGNMAVQQ VRAGLKAIYL SGWQVAGDAN LSGHTYPDQS LYPANSVPQV 

       130        140        150        160        170        180 
VRRINNALQR ADQIAKIEGD TSVENWLAPI VADGEAGFGG ALNVYELQKA LIAAGVAGSH 

       190        200        210        220        230        240 
WEDQLASEKK CGHLGGKVLI PTQQHIRTLT SARLAADVAD VPTVVIARTD AEAATLITSD 

       250        260        270        280        290        300 
VDERDQPFIT GERTREGFYR TKNGIEPCIA RAKAYAPFAD LIWMETGTPD LEAARQFSEA 

       310        320        330        340        350        360 
VKAEYPDQML AYNCSPSFNW KKHLDDATIA KFQKELAAMG FKFQFITLAG FHALNYSMFD 

       370        380        390        400        410        420 
LAYGYAQNQM SAYVELQERE FAAEERGYTA TKHQREVGAG YFDRIATTVD PNSSTTALTG 


STEEGQFH 

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis."
Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E., Gygi S.P., Darwin K.H.
PLoS ONE 5:E8589-E8589(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEASOME SUBSTRATE, PUPYLATION AT LYS-334, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: ATCC 25618 / H37Rv.
[3]"Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry."
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M., Kumar P. expand/collapse author list , Chaerkady R., Ramachandran S., Dash D., Pandey A.
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ATCC 25618 / H37Rv.
[4]"Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis."
Sharma V., Sharma S., zu Bentrup K.H., McKinney J.D., Russell D.G., Jacobs W.R. Jr., Sacchettini J.C.
Nat. Struct. Biol. 7:663-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL123456 Genomic DNA. Translation: CCP43200.1.
PIRG70828.
RefSeqYP_006513796.1. NC_018143.2.
YP_177728.1. NC_000962.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F61X-ray2.00A/B2-428[»]
1F8IX-ray2.25A/B/C/D2-428[»]
1F8MX-ray1.80A/B/C/D2-428[»]
ProteinModelPortalP9WKK7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID886291.

Organism-specific databases

TubercuListRv0467.

Phylogenomic databases

PhylomeDBP9WKK7.

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_MYCTU
AccessionPrimary (citable) accession number: P9WKK7
Secondary accession number(s): L0T3N9, O53752, P0A5H3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: July 9, 2014
This is version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names