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
Functions
4-hydroxy-4-methyl-2-oxoglutarate aldolase activity / metal ion binding / oxaloacetate decarboxylase activity / ribonuclease inhibitor activity
Processes
regulation 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
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
ResourceLink
UniProtKB IDP9WGY3
UniProtKB Entry NameRRAAH_MYCTU
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04343Glyoxylic acidexperimentalunknownDetails