Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase
Details
- Name
- Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase
- Synonyms
- 4.1.3.17
- HMG aldolase
- OAA decarboxylase
- Oxaloacetate decarboxylase
- Regulator of ribonuclease activity homolog
- RraA-like protein
- Gene Name
- rraA
- Organism
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- Amino acid sequence
>lcl|BSEQ0051203|Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase MAISFRPTADLVDDIGPDVRSCDLQFRQFGGRSQFAGPISTVRCFQDNALLKSVLSQPSA GGVLVIDGAGSLHTALVGDVIAELARSTGWTGLIVHGAVRDAAALRGIDIGIKALGTNPR KSTKTGAGERDVEITLGGVTFVPGDIAYSDDDGIIVV
- Number of residues
- 157
- Molecular Weight
- 16235.24
- Theoretical pI
- Not Available
- GO Classification
- Functions4-hydroxy-4-methyl-2-oxoglutarate aldolase activity / metal ion binding / oxaloacetate decarboxylase activity / ribonuclease inhibitor activityProcessesregulation of RNA metabolic process
- General Function
- Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions (By similarity).
- Specific Function
- 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity
- Pfam Domain Function
- RraA-like (PF03737)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0051204|Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase (rraA) GTGGCCATCTCATTTCGCCCAACCGCTGACCTCGTCGACGACATCGGGCCCGACGTGCGC AGCTGTGACCTACAGTTCCGCCAATTCGGCGGCCGATCGCAGTTCGCCGGACCGATCAGC ACCGTGCGGTGTTTTCAGGACAATGCGTTGCTGAAGTCGGTGCTCTCGCAGCCAAGTGCG GGCGGTGTGCTGGTCATCGACGGCGCCGGGTCCCTGCACACCGCGTTGGTCGGTGATGTC ATCGCCGAGTTGGCCCGCTCTACCGGCTGGACCGGGTTGATCGTCCACGGCGCGGTGCGA GATGCCGCCGCGCTGCGCGGCATCGACATCGGCATCAAAGCGCTGGGCACCAATCCCCGC AAGAGCACCAAGACCGGTGCCGGAGAACGCGACGTTGAAATCACGCTGGGCGGGGTGACA TTCGTTCCGGGCGATATCGCCTACAGCGACGACGACGGCATCATCGTCGTCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P9WGY3 UniProtKB Entry Name RRAAH_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]
- Raman K, Yeturu K, Chandra N: targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis. BMC Syst Biol. 2008 Dec 19;2:109. doi: 10.1186/1752-0509-2-109. [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]
- Johnston JM, Arcus VL, Morton CJ, Parker MW, Baker EN: Crystal structure of a putative methyltransferase from Mycobacterium tuberculosis: misannotation of a genome clarified by protein structural analysis. J Bacteriol. 2003 Jul;185(14):4057-65. [Article]