Isocitrate lyase
Details
- Name
- Isocitrate lyase
- Synonyms
- 4.1.3.1
- ICL
- Isocitrase
- Isocitratase
- Gene Name
- icl
- Organism
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- Amino acid sequence
>lcl|BSEQ0051124|Isocitrate lyase MSVVGTPKSAEQIQQEWDTNPRWKDVTRTYSAEDVVALQGSVVEEHTLARRGAEVLWEQL HDLEWVNALGALTGNMAVQQVRAGLKAIYLSGWQVAGDANLSGHTYPDQSLYPANSVPQV VRRINNALQRADQIAKIEGDTSVENWLAPIVADGEAGFGGALNVYELQKALIAAGVAGSH WEDQLASEKKCGHLGGKVLIPTQQHIRTLTSARLAADVADVPTVVIARTDAEAATLITSD VDERDQPFITGERTREGFYRTKNGIEPCIARAKAYAPFADLIWMETGTPDLEAARQFSEA VKAEYPDQMLAYNCSPSFNWKKHLDDATIAKFQKELAAMGFKFQFITLAGFHALNYSMFD LAYGYAQNQMSAYVELQEREFAAEERGYTATKHQREVGAGYFDRIATTVDPNSSTTALTG STEEGQFH
- Number of residues
- 428
- Molecular Weight
- 47086.255
- Theoretical pI
- Not Available
- GO Classification
- Functionsisocitrate lyase activity / metal ion binding / methylisocitrate lyase activity / zymogen bindingProcessescellular response to hypoxia / glyoxylate cycle / isocitrate metabolic process / maintenance of symbiont tolerance to host environment / pathogenesis / response to acetate / response to acid chemical / response to fatty acid / response to host immune response / tricarboxylic acid cycleComponentscytosol / extracellular region / plasma membrane
- General Function
- Involved in the persistence and virulence of M.tuberculosis. 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 (PubMed:10932251, PubMed:10963599, PubMed:18275086, PubMed:24354272). It could also catalyze the formation of pyruvate and succinate from 2-methylisocitrate, a key step in the methylcitrate cycle (propionate degradation route) (By similarity).
- Specific Function
- Isocitrate lyase activity
- Pfam Domain Function
- ICL (PF00463)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0051125|Isocitrate lyase (icl) ATGTCTGTCGTCGGCACCCCGAAGAGCGCGGAGCAGATCCAGCAGGAATGGGACACGAAC CCGCGCTGGAAGGACGTCACCCGCACCTACTCCGCCGAGGACGTCGTCGCCCTCCAGGGC AGCGTGGTCGAGGAGCACACGCTGGCCCGCCGCGGTGCGGAGGTGCTGTGGGAGCAGCTG CACGACCTCGAGTGGGTCAACGCGCTGGGCGCGCTGACCGGCAACATGGCCGTCCAGCAG GTGCGCGCCGGCCTGAAGGCCATCTACCTGTCGGGCTGGCAGGTCGCCGGCGATGCCAAC CTGTCCGGGCACACCTACCCCGACCAGAGCCTGTATCCCGCCAACTCGGTGCCGCAGGTG GTCCGCCGGATCAACAACGCACTGCAGCGCGCCGACCAGATCGCCAAGATCGAGGGCGAT ACTTCGGTGGAGAACTGGCTGGCGCCGATTGTCGCCGACGGCGAGGCCGGCTTTGGCGGC GCGCTCAACGTCTACGAGCTGCAGAAAGCCCTGATCGCCGCGGGCGTTGCGGGTTCGCAC TGGGAGGACCAGTTGGCCTCTGAGAAGAAGTGCGGCCACCTGGGCGGCAAGGTGTTGATC CCGACCCAGCAGCACATCCGCACTTTGACGTCTGCTCGGCTCGCGGCCGATGTGGCTGAT GTTCCCACGGTGGTGATCGCCCGTACCGACGCCGAGGCGGCCACGCTGATCACCTCCGAC GTCGACGAGCGCGACCAGCCGTTCATCACCGGCGAGCGCACCCGGGAAGGCTTCTACCGC ACCAAGAACGGCATCGAGCCTTGCATCGCTCGGGCGAAGGCCTACGCCCCGTTCGCCGAC TTGATCTGGATGGAGACCGGTACCCCGGACCTCGAGGCCGCCCGGCAGTTCTCCGAGGCG GTCAAGGCGGAGTACCCGGACCAGATGCTGGCCTACAACTGCTCGCCATCGTTCAACTGG AAAAAGCACCTCGACGACGCCACCATCGCCAAGTTCCAGAAGGAGCTGGCAGCCATGGGC TTCAAGTTCCAGTTCATCACGCTGGCCGGCTTCCATGCGCTGAACTACTCGATGTTCGAT CTGGCCTACGGCTACGCCCAGAACCAGATGAGCGCGTATGTCGAACTGCAGGAACGCGAG TTCGCCGCCGAAGAACGGGGCTACACCGCGACCAAGCACCAGCGCGAGGTCGGCGCCGGC TACTTCGACCGGATTGCCACCACCGTGGACCCGAATTCGTCGACCACCGCGTTGACCGGT TCCACCGAAGAGGGCCAGTTCCACTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P9WKK7 UniProtKB Entry Name ACEA_MYCTU - General References
- Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
- McKinney JD, Honer zu Bentrup K, Munoz-Elias EJ, Miczak A, Chen B, Chan WT, Swenson D, Sacchettini JC, Jacobs WR Jr, Russell DG: Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase. Nature. 2000 Aug 17;406(6797):735-8. [Article]
- Kumar R, Bhakuni V: Mycobacterium tuberculosis isocitrate lyase (MtbIcl): role of divalent cations in modulation of functional and structural properties. Proteins. 2008 Aug 15;72(3):892-900. doi: 10.1002/prot.21984. [Article]
- Festa RA, McAllister F, Pearce MJ, Mintseris J, Burns KE, Gygi SP, Darwin KH: Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis [corrected] . PLoS One. 2010 Jan 6;5(1):e8589. doi: 10.1371/journal.pone.0008589. [Article]
- Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
- Moynihan MM, Murkin AS: Cysteine is the general base that serves in catalysis by isocitrate lyase and in mechanism-based inhibition by 3-nitropropionate. Biochemistry. 2014 Jan 14;53(1):178-87. doi: 10.1021/bi401432t. Epub 2013 Dec 24. [Article]
- Sharma V, Sharma S, Hoener zu Bentrup K, McKinney JD, Russell DG, Jacobs WR Jr, Sacchettini JC: Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis. Nat Struct Biol. 2000 Aug;7(8):663-8. [Article]
- Micklinghoff JC, Breitinger KJ, Schmidt M, Geffers R, Eikmanns BJ, Bange FC: Role of the transcriptional regulator RamB (Rv0465c) in the control of the glyoxylate cycle in Mycobacterium tuberculosis. J Bacteriol. 2009 Dec;191(23):7260-9. doi: 10.1128/JB.01009-09. Epub 2009 Sep 18. [Article]
- Masiewicz P, Brzostek A, Wolanski M, Dziadek J, Zakrzewska-Czerwinska J: A novel role of the PrpR as a transcription factor involved in the regulation of methylcitrate pathway in Mycobacterium tuberculosis. PLoS One. 2012;7(8):e43651. doi: 10.1371/journal.pone.0043651. Epub 2012 Aug 16. [Article]