{"metadata":{"accession":"PF11623","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR021659","hierarchy":null,"name":{"name":"NAD(P)H dehydrogenase subunit S","short":"NdhS"},"description":[{"text":"<p>This family is found in Bacteria and Streptophyta includes members such as NdhS (NAD(P)H-quinone oxidoreductase subunit S). NdhS, also known as CRR31 (chlororespiratory reduction 31), is a subunit of the chloroplast NADH dehydrogenase-like (NDH) complex [[cite:PUB00083363]]. It is also a subunit of the cyanobacterial NDH-1 complex [[cite:PUB00083366]] [[cite:PUB00083365]]. NAD(P)H-oxidizing subunits have not been found in chloroplasts or cyanobacteria, where ferredoxin is probably the electron donor. NdhS contributes to the formation of a ferredoxin binding site of NDH [[cite:PUB00083363]] and is necessary for high affinity binding of ferredoxin [[cite:PUB00083368]]. The cyanobacterial NDH-1 complex, also known as NADPH:plastoquinone oxidoreductase or type I NAD(P)H dehydrogenase, is involved in plastoquinone reduction and cyclic electron transfer (CET) around photosystem I. The chloroplast NDH is more similar to cyanobacterial NDH-1, which is believed to be the origin of chloroplast NDH, than to mitochondrial NADH dehydrogenase present in the same species [[cite:PUB00083364]] [[cite:PUB00083367]]. The NDH complexes of chloroplasts, however, contain many subunits that are absent from cyanobacterial NDH-1 complexes.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00083364":{"PMID":21785130,"ISBN":null,"volume":"52","issue":"9","year":2011,"title":"Structure of the chloroplast NADH dehydrogenase-like complex: nomenclature for nuclear-encoded subunits.","URL":null,"raw_pages":"1560-8","medline_journal":"Plant Cell Physiol","ISO_journal":"Plant Cell Physiol.","authors":["Ifuku K","Endo T","Shikanai T","Aro EM."],"DOI_URL":"http://dx.doi.org/10.1093/pcp/pcr098"},"PUB00083363":{"PMID":21505067,"ISBN":null,"volume":"23","issue":"4","year":2011,"title":"An Src homology 3 domain-like fold protein forms a ferredoxin binding site for the chloroplast NADH dehydrogenase-like complex in Arabidopsis.","URL":null,"raw_pages":"1480-93","medline_journal":"Plant Cell","ISO_journal":"Plant Cell","authors":["Yamamoto H","Peng L","Fukao Y","Shikanai T."],"DOI_URL":"http://dx.doi.org/10.1105/tpc.110.080291"},"PUB00083367":{"PMID":21035426,"ISBN":null,"volume":"1807","issue":"8","year":2011,"title":"Cyanobacterial NDH-1 complexes: novel insights and remaining puzzles.","URL":null,"raw_pages":"935-44","medline_journal":"Biochim Biophys Acta","ISO_journal":"Biochim. Biophys. Acta","authors":["Battchikova N","Eisenhut M","Aro EM."],"DOI_URL":"http://dx.doi.org/10.1016/j.bbabio.2010.10.017"},"PUB00083365":{"PMID":25630976,"ISBN":null,"volume":"126","issue":"2-3","year":2015,"title":"NDH-1L interacts with ferredoxin via the subunit NdhS in Thermosynechococcus elongatus.","URL":null,"raw_pages":"341-9","medline_journal":"Photosynth Res","ISO_journal":"Photosyn. Res.","authors":["He Z","Zheng F","Wu Y","Li Q","Lv J","Fu P","Mi H."],"DOI_URL":"http://dx.doi.org/10.1007/s11120-015-0090-4"},"PUB00083368":{"PMID":24225949,"ISBN":null,"volume":"288","issue":"51","year":2013,"title":"In planta mutagenesis of Src homology 3 domain-like fold of NdhS, a ferredoxin-binding subunit of the chloroplast NADH dehydrogenase-like complex in Arabidopsis: a conserved Arg-193 plays a critical role in ferredoxin binding.","URL":null,"raw_pages":"36328-37","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Yamamoto H","Shikanai T."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M113.511584"},"PUB00083366":{"PMID":21880717,"ISBN":null,"volume":"286","issue":"42","year":2011,"title":"Identification of novel Ssl0352 protein (NdhS), essential for efficient operation of cyclic electron transport around photosystem I, in NADPH:plastoquinone oxidoreductase (NDH-1) complexes of Synechocystis sp. PCC 6803.","URL":null,"raw_pages":"36992-7001","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Battchikova N","Wei L","Du L","Bersanini L","Aro EM","Ma W."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M111.263780"}},"set_info":{"accession":"CL0010","name":"SH3"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":8,"interactions":0,"matches":721,"pathways":0,"proteins":721,"proteomes":581,"sets":1,"structural_models":{"alphafold":546},"structures":12,"taxa":1686},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":21,"alignment:full":482},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"3c4s","name":"Crystal structure of the Ssl0352 protein from Synechocystis sp. Northeast Structural Genomics Consortium target SgR42"}}}