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{
"metadata": {
"accession": "IPR036514",
"entry_id": null,
"type": "homologous_superfamily",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"cathgene3d": {
"G3DSA:3.40.50.1110": "SGNH hydrolase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR036514",
"name": "SGNH hydrolase superfamily",
"type": "Homologous_superfamily",
"children": []
},
"name": {
"name": "SGNH hydrolase superfamily",
"short": "SGNH_hydro_sf"
},
"description": [
{
"text": "<p>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:PUB00019795], [cite:PUB00033179]]. 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 [[cite:PUB00033174]]; the esterase domain of viral haemagglutinin-esterase surface glycoproteins (influenza C virus, coronaviruses and toroviruses) [[cite:PUB00010667]]; mammalian acetylhydrolases [[cite:PUB00021627]]; fungal rhamnogalacturonan acetylesterase [[cite:PUB00026651]]; and the multifunctional enzyme thioesterase I (TAP) from Escherichia coli [[cite:PUB00026145]]. SGNH hydrolase-type esterase domains contain unique hydrogen bond network that stabilises their catalytic centres; they usually contain the catalytic triad Ser/Acid/His [[cite:PUB00097376]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00019795": {
"PMID": 10801485,
"ISBN": null,
"volume": "8",
"issue": "4",
"year": 2000,
"title": "Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases.",
"URL": null,
"raw_pages": "373-83",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Molgaard A",
"Kauppinen S",
"Larsen S."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(00)00118-0"
},
"PUB00033179": {
"PMID": 15522763,
"ISBN": null,
"volume": "43",
"issue": "6",
"year": 2004,
"title": "GDSL family of serine esterases/lipases.",
"URL": null,
"raw_pages": "534-52",
"medline_journal": "Prog Lipid Res",
"ISO_journal": "Prog. Lipid Res.",
"authors": [
"Akoh CC",
"Lee GC",
"Liaw YC",
"Huang TH",
"Shaw JF."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.plipres.2004.09.002"
},
"PUB00026651": {
"PMID": 11752785,
"ISBN": null,
"volume": "58",
"issue": "Pt 1",
"year": 2002,
"title": "A branched N-linked glycan at atomic resolution in the 1.12 A structure of rhamnogalacturonan acetylesterase.",
"URL": null,
"raw_pages": "111-9",
"medline_journal": "Acta Crystallogr D Biol Crystallogr",
"ISO_journal": "Acta Crystallogr. D Biol. Crystallogr.",
"authors": [
"Molgaard A",
"Larsen S."
],
"DOI_URL": null
},
"PUB00033174": {
"PMID": 7773790,
"ISBN": null,
"volume": "2",
"issue": "3",
"year": 1995,
"title": "A novel variant of the catalytic triad in the Streptomyces scabies esterase.",
"URL": null,
"raw_pages": "218-23",
"medline_journal": "Nat Struct Biol",
"ISO_journal": "Nat. Struct. Biol.",
"authors": [
"Wei Y",
"Schottel JL",
"Derewenda U",
"Swenson L",
"Patkar S",
"Derewenda ZS."
],
"DOI_URL": "http://dx.doi.org/10.1038/nsb0395-218"
},
"PUB00021627": {
"PMID": 11522926,
"ISBN": null,
"volume": "14",
"issue": "7",
"year": 2001,
"title": "Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib.",
"URL": null,
"raw_pages": "513-9",
"medline_journal": "Protein Eng",
"ISO_journal": "Protein Eng.",
"authors": [
"Sheffield PJ",
"McMullen TW",
"Li J",
"Ho YS",
"Garrard SM",
"Derewenda U",
"Derewenda ZS."
],
"DOI_URL": "http://dx.doi.org/10.1093/protein/14.7.513"
},
"PUB00010667": {
"PMID": 9817207,
"ISBN": null,
"volume": "396",
"issue": "6706",
"year": 1998,
"title": "Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus.",
"URL": null,
"raw_pages": "92-6",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Rosenthal PB",
"Zhang X",
"Formanowski F",
"Fitz W",
"Wong CH",
"Meier-Ewert H",
"Skehel JJ",
"Wiley DC."
],
"DOI_URL": "http://dx.doi.org/10.1038/23974"
},
"PUB00026145": {
"PMID": 12842470,
"ISBN": null,
"volume": "330",
"issue": "3",
"year": 2003,
"title": "Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network.",
"URL": null,
"raw_pages": "539-51",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Lo YC",
"Lin SC",
"Shaw JF",
"Liaw YC."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0022-2836(03)00637-5"
},
"PUB00097376": {
"PMID": 28558229,
"ISBN": null,
"volume": "12",
"issue": "7",
"year": 2017,
"title": "Catalytic Dyad in the SGNH Hydrolase Superfamily: In-depth Insight into Structural Parameters Tuning the Catalytic Process of Extracellular Lipase from Streptomyces rimosus.",
"URL": null,
"raw_pages": "1928-1936",
"medline_journal": "ACS Chem Biol",
"ISO_journal": "ACS Chem Biol",
"authors": [
"Lescic Asler I",
"Stefanic Z",
"Marsavelski A",
"Vianello R",
"Kojic-Prodic B."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR001087",
"name": "GDSL lipase/esterase",
"type": "family"
},
{
"accession": "IPR013830",
"name": "SGNH hydrolase-type esterase domain",
"type": "domain"
},
{
"accession": "IPR007407",
"name": "Protein of unknown function DUF459",
"type": "family"
},
{
"accession": "IPR005181",
"name": "Sialate O-acetylesterase domain",
"type": "domain"
},
{
"accession": "IPR035547",
"name": "Phospholipase B",
"type": "domain"
},
{
"accession": "IPR035669",
"name": "GDSL lipase/esterase-like, plant",
"type": "family"
},
{
"accession": "IPR033447",
"name": "OSK domain",
"type": "domain"
},
{
"accession": "IPR032616",
"name": "Domain of unknown function DUF4886",
"type": "domain"
},
{
"accession": "IPR032588",
"name": "Putative GDSL-like Lipase/Acylhydrolase",
"type": "family"
},
{
"accession": "IPR016948",
"name": "Uncharacterised conserved protein UCP030175",
"type": "family"
},
{
"accession": "IPR053140",
"name": "GDSL lipase Rv0518-like",
"type": "family"
},
{
"accession": "IPR051532",
"name": "Diverse Ester Hydrolysis Enzymes",
"type": "family"
},
{
"accession": "IPR037460",
"name": "Streptomyces scabies esterase-like",
"type": "family"
},
{
"accession": "IPR045136",
"name": "Isoamyl acetate-hydrolyzing esterase Iah1-like",
"type": "family"
},
{
"accession": "IPR037459",
"name": "Rhamnogalacturonan acetylesterase RhgT-like",
"type": "family"
},
{
"accession": "IPR037461",
"name": "CtCE2-like domain",
"type": "domain"
},
{
"accession": "IPR052762",
"name": "Plant cell wall deacetylase/carbohydrate esterase",
"type": "family"
},
{
"accession": "IPR051058",
"name": "GDSL Esterase/Lipase Enzyme",
"type": "family"
},
{
"accession": "IPR044552",
"name": "GDSL esterase/lipase GLIP1-5/GLL25",
"type": "family"
},
{
"accession": "IPR050592",
"name": "GDSL lipolytic enzyme",
"type": "family"
},
{
"accession": "IPR049369",
"name": "BF1531-like, N-terminal domain",
"type": "domain"
},
{
"accession": "IPR055041",
"name": "Peptidoglycan O-acetylesterase, N-terminal",
"type": "domain"
},
{
"accession": "IPR051238",
"name": "GDSL esterase/lipase",
"type": "family"
},
{
"accession": "IPR052940",
"name": "Carbohydrate Esterase 6",
"type": "family"
},
{
"accession": "IPR054624",
"name": "GDSL lipase Rv0518",
"type": "family"
},
{
"accession": "IPR050023",
"name": "Diglucosylglycerate octanoyltransferase",
"type": "family"
},
{
"accession": "IPR057572",
"name": "Non-GDSL lipase-like",
"type": "family"
},
{
"accession": "IPR050040",
"name": "Acetylxylan esterase/glucomannan deacetylase",
"type": "family"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 271502,
"pathways": 17,
"proteins": 260223,
"proteomes": 20119,
"sets": 0,
"structural_models": {
"alphafold": 201377,
"bfvd": 146
},
"structures": 208,
"taxa": 37995
},
"entry_annotations": {},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "3.1.1",
"url": "https://enzyme.expasy.org/EC/3.1.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "5tif",
"name": "x-ray structure of acyl-CoA thioesterase I, TesA, triple mutant M141L/Y145K/L146K in complex with octanoic acid"
}
}
}
