Protein Family Models

This family has an alpha/beta topology, with 13 conserved hydrophobic residues at its core and a putative active site containing a highly conserved cysteine [1]. Members of this family are involved in a range of physiological functions. The family includes PaaJ (PhaH) Swiss:O84984 from Pseudomonas putida. PaaJ forms a complex with PaaG (PhaF) Swiss:O84982, PaaI (PhaG) Swiss:O84983 and PaaK (PhaI) Swiss:O84985, which hydroxylates phenylacetic acid to 2-hydroxyphenylacetic acid [2]. It also includes PaaD Swiss:P76080 from Escherichia coli, a member of a multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation [3]. Furthermore, several members of this family are shown to be involved in iron-sulfur (FeS) cluster assembly. Iron-sulfur (FeS) clusters are inorganic co-factors that are are able to transfer electrons and act as catalysts [4]. They are involved in diverse cellular processes including cellular respiration, DNA replication and repair, antibiotic resistance, and dinitrogen fixation [5]. The biogenesis of such clusters from elemental iron and sulfur is an enzymatic process that requires a set of specialised proteins. Proteins containing this domain include the chloroplast protein HCF101 (high chlorophyll fluorescence 101), Swiss:Q6STH5, which has been described as an essential and specific factor for assembly of [4Fe-4S]-cluster-containing protein complexes such as the membrane complex Photosystem I (PSI) and the heterodimeric FTR (ferredoxin-thioredoxin reductase) complex [4] and is involved in the assembly of [4Fe-4S] clusters and their transfer to apoproteins [4]. The mature HCF101 protein contains this do. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14