This domain is found at the C-terminal end of the probable enoyl -CoA hydratase alpha subunit from Thermomonospora curvata (ChsH2) and similar archaeal and bacterial proteins. ChsH2 is likely to be involved in bile acid degradation. The C-terminal region of this protein is organised into two domains: an N-terminal zinc finger domain ([pfam:PF12172]) and an OB-fold domain (this entry) that consists of a five-stranded beta-barrel [[cite:PUB00155451]]. This domain is also found in 3-oxo-4,17- pregnadiene-20-carboxyl-CoA hydratase alpha subunit from Mycobacterium tuberculosis that is involved in cholesterol side chain degradation [[cite:PUB00154876]]. It is also found in Methanothermococcus thermolithotrophicus HMGCS, an enzyme complex comprising the thiolase and 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase, that catalyses the second reaction in the mevalonate pathway-the exergonic condensation of acetoacetyl-CoA and acetyl-CoA to HMG-CoA [[cite:PUB00154878]].
","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00159916":{"PMID":30318713,"ISBN":null,"volume":"20","issue":"1","year":2019,"title":"Structure and Catalytic Mechanism of a Bacterial Friedel-Crafts Acylase.","URL":null,"raw_pages":"88-95","medline_journal":"Chembiochem","ISO_journal":"Chembiochem","authors":["Pavkov-Keller T","Schmidt NG","Zadlo-Dobrowolska A","Kroutil W","Gruber K."],"DOI_URL":"https://doi.org/10.1002/cbic.201800462"},"PUB00070339":{"PMID":23793631,"ISBN":null,"volume":"79","issue":"17","year":2013,"title":"Haloarchaeal-type β-ketothiolases involved in Poly(3-hydroxybutyrate-co-3-hydroxyvalerate) synthesis in Haloferax mediterranei.","URL":null,"raw_pages":"5104-11","medline_journal":"Appl Environ Microbiol","ISO_journal":"Appl. Environ. Microbiol.","authors":["Hou J","Feng B","Han J","Liu H","Zhao D","Zhou J","Xiang H."],"DOI_URL":"http://dx.doi.org/10.1128/AEM.01370-13"},"PUB00154878":{"PMID":29531083,"ISBN":null,"volume":"115","issue":"13","year":2018,"title":"Archaeal acetoacetyl-CoA thiolase/HMG-CoA synthase complex channels the intermediate via a fused CoA-binding site.","URL":null,"raw_pages":"3380-3385","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc Natl Acad Sci U S A","authors":["Vogeli B","Engilberge S","Girard E","Riobe F","Maury O","Erb TJ","Shima S","Wagner T."],"DOI_URL":"https://doi.org/10.1073/pnas.1718649115"},"PUB00154876":{"PMID":25203216,"ISBN":null,"volume":"9","issue":"11","year":2014,"title":"A distinct MaoC-like enoyl-CoA hydratase architecture mediates cholesterol catabolism in Mycobacterium tuberculosis.","URL":null,"raw_pages":"2632-45","medline_journal":"ACS Chem Biol","ISO_journal":"ACS Chem Biol","authors":["Yang M","Guja KE","Thomas ST","Garcia-Diaz M","Sampson NS."],"DOI_URL":"https://doi.org/10.1021/cb500232h"},"PUB00155451":{"PMID":31209106,"ISBN":null,"volume":"294","issue":"31","year":2019,"title":"The steroid side-chain-cleaving aldolase Ltp2-ChsH2DUF35 is a thiolase superfamily member with a radically repurposed active site.","URL":null,"raw_pages":"11934-11943","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Aggett R","Mallette E","Gilbert SE","Vachon MA","Schroeter KL","Kimber MS","Seah SYK."],"DOI_URL":"https://doi.org/10.1074/jbc.RA119.008889"},"PUB00097287":{"PMID":20944206,"ISBN":null,"volume":"66","issue":"Pt 10","year":2010,"title":"The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding role.","URL":null,"raw_pages":"1160-6","medline_journal":"Acta Crystallogr Sect F Struct Biol Cryst Commun","ISO_journal":"Acta Crystallogr Sect F Struct Biol Cryst Commun","authors":["Krishna SS","Aravind L","Bakolitsa C","Caruthers J","Carlton D","Miller MD","Abdubek P","Astakhova T","Axelrod HL","Chiu HJ","Clayton T","Deller MC","Duan L","Feuerhelm J","Grant JC","Han GW","Jaroszewski L","Jin KK","Klock HE","Knuth MW","Kumar A","Marciano D","McMullan D","Morse AT","Nigoghossian E","Okach L","Reyes R","Rife CL","van den Bedem H","Weekes D","Xu Q","Hodgson KO","Wooley J","Elsliger MA","Deacon AM","Godzik A","Lesley SA","Wilson IA."],"DOI_URL":null}},"set_info":{"accession":"CL0021","name":"OB"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":41,"interactions":0,"matches":16307,"pathways":0,"proteins":14915,"proteomes":4357,"sets":1,"structural_models":{"alphafold":9479},"structures":12,"taxa":6361},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":70,"alignment:full":7657},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}