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. 2011 Jan 25;286(13):10930–10938. doi: 10.1074/jbc.M110.216127

TABLE 1.

Properties of OleA compared with homologous proteins in the thiolase superfamily

Protein (organism)a Accession number Sequence identityb Calculated Mr Calculated pI Cellular function Claisen mechanism Sequence signaturec
%
OleA (X. campestris) NP_635607 100 36,629 5.6 Alkene biosynthesis Proposed NACLAFING
Non-decarboxylative
OleA (M. luteus) (11) YP_002957382.1 38 36,653 4.8 Alkene biosynthesis Proposed decarboxylative NACLGFVNG
Thiolase (Zoogloea ramigera) (23) AAA27706.1 19 40,416 5.9 PHB biosynthesis Non-decarboxylative QLCGSGLRA
HMG-CoA synthase (Homo sapiens) (26) 1XPL_A 16 43,204 5.0 Mevalonate pathway Non-decarboxylative EACYAATPA
FabH (E. coli) (25) 1EBL_A 24 33,523 5.1 Fatty acid biosynthesis Decarboxylative AACAGFTYA
Mycobacterium Pks13d (24) CAA17864 19 44,122 5.2 Mycolic acid biosynthesis Decarboxylative TACSSSLVA

a Numbers in this column represent references from which the data in the table were obtained.

b Via Needleman-Wunch and BLAST algorithms and comparison with OleA from X. campestris.

c Amino acid sequence surrounding the active site cysteine conserved in thiolase superfamily proteins.

d Alignment to keto-acyl synthase domain only, as defined by NCBI.