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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR004131",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0004427",
"name": "inorganic diphosphate phosphatase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0009678",
"name": "diphosphate hydrolysis-driven proton transmembrane transporter activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:1902600",
"name": "proton transmembrane transport",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"identifier": "GO:0016020",
"name": "membrane",
"category": {
"code": "C",
"name": "cellular_component"
}
}
],
"source_database": "interpro",
"member_databases": {
"panther": {
"PTHR31998": "K(+)-INSENSITIVE PYROPHOSPHATE-ENERGIZED PROTON PUMP"
},
"hamap": {
"MF_01129": "Putative K(+)-stimulated pyrophosphate-energized sodium pump [hppA]"
},
"pfam": {
"PF03030": "Inorganic H+ pyrophosphatase"
},
"pirsf": {
"PIRSF001265": "H(+)-translocating inorganic pyrophosphatase"
},
"ncbifam": {
"TIGR01104": "V-type H(+)-translocating pyrophosphatase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR004131",
"name": "Pyrophosphate-energised proton pump",
"type": "Family",
"children": []
},
"name": {
"name": "Pyrophosphate-energised proton pump",
"short": "PPase-energised_H-pump"
},
"description": [
{
"text": "<p>Two types of proteins that hydrolyse inorganic pyrophosphate (PPi), very different in both amino acid sequence and structure, have been characterised to date: soluble and membrane-bound proton-pumping pyrophosphatases (sPPases and H+)-PPases, respectively). sPPases are ubiquitous proteins that hydrolyse PPi to release heat, whereas H+-PPases, so far unidentified in animal and fungal cells, couple the energy of PPi hydrolysis to proton movement across biological membranes [[cite:PUB00014387]]. The latter type is represented by this group of proteins. H+-PPases ([ec:3.6.1.1]) are also called vacuolar-type inorganic pyrophosphatases (V-PPase) or pyrophosphate-energised vacuolar membrane proton pumps [[cite:PUB00014458]]. In plants, vacuoles contain two enzymes for acidifying the interior of the vacuole, the V-ATPase and the V-PPase (V is for vacuolar) [[cite:PUB00014387]]. In Arabidopsis, AVP1 contributes to H+-electrochemical potential difference between the citosol and vacuole lumen and also facilitates auxin transport by modulating apoplastic pH and regulates auxin-mediated developmental processes [[cite:PUB00097876]].</p>\n\n<p>Two distinct biochemical subclasses of H+-PPases have been characterised to date: K+-stimulated and K+-insensitive [[cite:PUB00014458]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00014458": {
"PMID": 11343697,
"ISBN": null,
"volume": "496",
"issue": "1",
"year": 2001,
"title": "A thermostable K(+)-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima.",
"URL": null,
"raw_pages": "6-11",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Perez-Castineira JR",
"Lopez-Marques RL",
"Losada M",
"Serrano A."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0014-5793(01)02390-0"
},
"PUB00014387": {
"PMID": 10523139,
"ISBN": null,
"volume": "457",
"issue": "3",
"year": 1999,
"title": "H+ -PPases: a tightly membrane-bound family.",
"URL": null,
"raw_pages": "527-33",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Baltscheffsky M",
"Schultz A",
"Baltscheffsky H."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0014-5793(99)90617-8"
},
"PUB00097876": {
"PMID": 16210544,
"ISBN": null,
"volume": "310",
"issue": "5745",
"year": 2005,
"title": "Arabidopsis H+-PPase AVP1 regulates auxin-mediated organ development.",
"URL": null,
"raw_pages": "121-5",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Li J",
"Yang H",
"Peer WA",
"Richter G",
"Blakeslee J",
"Bandyopadhyay A",
"Titapiwantakun B",
"Undurraga S",
"Khodakovskaya M",
"Richards EL",
"Krizek B",
"Murphy AS",
"Gilroy S",
"Gaxiola R",
"Richter G",
"Gilroy S."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 170,
"interactions": 0,
"matches": 18215,
"pathways": 0,
"proteins": 18026,
"proteomes": 8548,
"sets": 0,
"structural_models": {
"alphafold": 14512,
"bfvd": 0
},
"structures": 22,
"taxa": 16245
},
"entry_annotations": {
"alignment:seed": 223,
"alignment:full": 8309
},
"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": "7.1.3.1",
"url": "https://enzyme.expasy.org/EC/7.1.3.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
