SGNH hydrolase superfamily

Definition

SGNH hydrolase has a similar fold to flavoproteins, namely a three-layer α/β/α structure, where the β-sheets are composed of five parallel strands. Enzymes containing this domain act as esterases and lipases, but have little sequence homology to true lipases [[cite:PMID:10801485], [cite:PMID:15522763]]. Proteins containing this type of esterase domain have been found in a variety of hydrolases; those with structural information include an esterase from Streptomyces scabies PMID:7773790; the esterase domain of viral haemagglutinin-esterase surface glycoproteins (influenza C virus, coronaviruses and toroviruses) PMID:9817207; mammalian acetylhydrolases PMID:11522926; fungal rhamnogalacturonan acetylesterase PMID:11752785; and the multifunctional enzyme thioesterase I (TAP) from Escherichia coli PMID:12842470. SGNH hydrolase-type esterase domains contain unique hydrogen bond network that stabilises their catalytic centres; they usually contain the catalytic triad Ser/Acid/His PMID:28558229.

7 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (7 proteins: gene, accession, name)

• AOAH
• IAH1
• PAFAH1B2
• PAFAH1B3
• PCED1B
• PLB1
• SIAE