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Protein

Isocitrate lyase 1

Gene

icl

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Involved in the persistence and virulence of Mycobacterium. 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.1 Publication

Catalytic activityi

Isocitrate = succinate + glyoxylate.By similarity

Cofactori

Mg2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi153 – 1531MagnesiumBy similarity
Active sitei191 – 1911Proton acceptorBy similarity
Binding sitei228 – 2281SubstrateBy similarity
Binding sitei347 – 3471SubstrateBy similarity

GO - Molecular functioni

  1. isocitrate lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. glyoxylate cycle Source: UniProtKB-UniPathway
  2. 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

UniPathwayiUPA00703; UER00719.

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate lyase 11 Publication (EC:4.1.3.1By similarity)
Short name:
ICL11 Publication
Alternative name(s):
Isocitrase1 Publication
Isocitratase1 Publication
Gene namesi
Name:icl
Ordered Locus Names:Mb0476
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001419 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

cells lacking this gene show a slight residual isocitrate lyase activity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Isocitrate lyase 1PRO_0000068777Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi233413.Mb0476.

Structurei

3D structure databases

ProteinModelPortaliP0A5H4.
SMRiP0A5H4. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni91 – 933Substrate bindingBy similarity
Regioni192 – 1932Substrate bindingBy similarity
Regioni313 – 3175Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2224.
HOGENOMiHOG000238475.
KOiK01637.
OMAiRWKGVTR.
OrthoDBiEOG689HMX.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamiPF00463. ICL. 1 hit.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR01346. isocit_lyase. 2 hits.
PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A5H4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVVGTPKSA EQIQQEWDTN PRWKDVTRTY SAEDVVALQG SVVEEHTLAR
60 70 80 90 100
RGAEVLWEQL HDLEWVNALG ALTGNMAVQQ VRAGLKAIYL SGWQVAGDAN
110 120 130 140 150
LSGHTYPDQS LYPANSVPQV VRRINNALQR ADQIAKIEGD TSVENWLAPI
160 170 180 190 200
VADGEAGFGG ALNVYELQKA LIAAGVAGSH WEDQLASEKK CGHLGGKVLI
210 220 230 240 250
PTQQHIRTLT SARLAADVAD VPTVVIARTD AEAATLITSD VDERDQPFIT
260 270 280 290 300
GERTREGFYR TKNGIEPCIA RAKAYAPFAD LIWMETGTPD LEAARQFSEA
310 320 330 340 350
VKAEYPDQML AYNCSPSFNW KKHLDDATIA KFQKELAAMG FKFQFITLAG
360 370 380 390 400
FHALNYSMFD LAYGYAQNQM SAYVELQERE FAAEERGYTA TKHQREVGAG
410 420
YFDRIATTVD PNSSTTALTG STEEGQFH
Length:428
Mass (Da):47,087
Last modified:March 14, 2005 - v1
Checksum:iE5223F38CB5D9E8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248333 Genomic DNA. Translation: CDO41716.1.
RefSeqiNP_854139.1. NC_002945.3.

Genome annotation databases

EnsemblBacteriaiCDO41716; CDO41716; Mb0476.
GeneIDi1091513.
KEGGimbo:Mb0476.
PATRICi18002699. VBIMycBov88188_0518.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248333 Genomic DNA. Translation: CDO41716.1.
RefSeqiNP_854139.1. NC_002945.3.

3D structure databases

ProteinModelPortaliP0A5H4.
SMRiP0A5H4. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi233413.Mb0476.

Chemistry

BindingDBiP0A5H4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCDO41716; CDO41716; Mb0476.
GeneIDi1091513.
KEGGimbo:Mb0476.
PATRICi18002699. VBIMycBov88188_0518.

Phylogenomic databases

eggNOGiCOG2224.
HOGENOMiHOG000238475.
KOiK01637.
OMAiRWKGVTR.
OrthoDBiEOG689HMX.

Enzyme and pathway databases

UniPathwayiUPA00703; UER00719.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamiPF00463. ICL. 1 hit.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR01346. isocit_lyase. 2 hits.
PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-935 / AF2122/97.
  2. "13C metabolic flux analysis identifies an unusual route for pyruvate dissimilation in mycobacteria which requires isocitrate lyase and carbon dioxide fixation."
    Beste D.J., Bonde B., Hawkins N., Ward J.L., Beale M.H., Noack S., Noeh K., Kruger N.J., Ratcliffe R.G., McFadden J.
    PLoS Pathog. 7:E1002091-E1002091(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiACEA1_MYCBO
AccessioniPrimary (citable) accession number: P0A5H4
Secondary accession number(s): O53752, X2BF40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 14, 2005
Last sequence update: March 14, 2005
Last modified: March 31, 2015
This is version 65 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

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.