Poecilia_mexicanaFamily: Aconitase_C Number of Genes: 4
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
ireb2
aco2
aco1
ACO2 (1 of many)

Introduction

Pfam

Members of this family usually also match to PF00330. This domain undergoes conformational change in the enzyme mechanism [1].

InterPro

Aconitase (aconitate hydratase; EC) is an iron-sulphur protein that contains a [4Fe-4S]-cluster and catalyses the interconversion of isocitrate and citrate via a cis-aconitate intermediate. Aconitase functions in both the TCA and glyoxylate cycles, however unlike the majority of iron-sulphur proteins that function as electron carriers, the [4Fe-4S]-cluster of aconitase reacts directly with an enzyme substrate. In eukaryotes there is a cytosolic form (cAcn) and a mitochondrial form (mAcn) of the enzyme. In bacteria there are also 2 forms, aconitase A (AcnA) and B (AcnB). Several aconitases are known to be multi-functional enzymes with a second non-catalytic, but essential function that arises when the cellular environment changes, such as when iron levels drop [PUBMED:10087914, PUBMED:15877277]. Eukaryotic cAcn and mAcn, and bacterial AcnA have the same domain organisation, consisting of three N-terminal alpha/beta/alpha domains, a linker region, followed by a C-terminal 'swivel' domain with a beta/beta/alpha structure (1-2-3-linker-4), although mAcn is small than cAcn. However, bacterial AcnB has a different organisation: it contains an N-terminal HEAT-like domain, followed by the 'swivel' domain, then the three alpha/beta/alpha domains (HEAT-4-1-2-3) [PUBMED:9020582].

Reference

  1. Lauble H, Stout CD; , Proteins 1995;22:1-11.: Steric and conformational features of the aconitase mechanism. PUBMED:7675781 EPMC:7675781.