登録情報 | データベース: PDB / ID: 4gox |
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タイトル | Sulfotransferase Domain from the Synechococcus PCC 7002 Olefin Synthase |
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要素 | Polyketide synthase |
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キーワード | TRANSFERASE / olefin synthase / polyketide synthase / hydrocarbon / sulfotransferase / PAPS / PAP / 3'phosphoadenosine-5'phosphosulfate |
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機能・相同性 | 機能・相同性情報
DIM/DIP cell wall layer assembly / secondary metabolite biosynthetic process / fatty acid synthase activity / phosphopantetheine binding / 3-oxoacyl-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process / nucleotide binding / plasma membrane / cytoplasm類似検索 - 分子機能 Sulfotransferase family / Fatty acyl-AMP ligase /fatty acyl-CoA ligase / PKS_PP_betabranch / : / Polyketide synthase, ketoreductase domain / KR domain / Polyketide synthase, C-terminal extension / Ketoacyl-synthetase C-terminal extension / ANL, N-terminal domain / PKS_KR ...Sulfotransferase family / Fatty acyl-AMP ligase /fatty acyl-CoA ligase / PKS_PP_betabranch / : / Polyketide synthase, ketoreductase domain / KR domain / Polyketide synthase, C-terminal extension / Ketoacyl-synthetase C-terminal extension / ANL, N-terminal domain / PKS_KR / Acyl transferase domain superfamily / Acyl transferase / Acyl transferase domain / Acyl transferase domain in polyketide synthase (PKS) enzymes. / AMP-binding, conserved site / Putative AMP-binding domain signature. / Acyl transferase/acyl hydrolase/lysophospholipase / Epoxide hydrolase-like / Ketosynthase family 3 (KS3) domain profile. / Polyketide synthase, phosphopantetheine-binding domain / Phosphopantetheine attachment site / AMP-dependent synthetase/ligase / AMP-binding enzyme, C-terminal domain superfamily / AMP-binding enzyme / Beta-ketoacyl synthase / Beta-ketoacyl synthase, active site / Ketosynthase family 3 (KS3) active site signature. / Polyketide synthase, beta-ketoacyl synthase domain / Beta-ketoacyl synthase, N-terminal / Beta-ketoacyl synthase, C-terminal / Beta-ketoacyl synthase, N-terminal domain / Beta-ketoacyl synthase, C-terminal domain / alpha/beta hydrolase fold / Alpha/beta hydrolase fold-1 / Thiolase-like / Phosphopantetheine attachment site / Phosphopantetheine attachment site. / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Alpha/Beta hydrolase fold / P-loop containing nucleotide triphosphate hydrolases / NAD(P)-binding domain superfamily / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Alpha Beta類似検索 - ドメイン・相同性 ADENOSINE-3'-5'-DIPHOSPHATE / Polyketide synthase類似検索 - 構成要素 |
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生物種 | Synechococcus sp. (バクテリア) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 2.15 Å |
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データ登録者 | McCarthy, J.G. / Smith, J.L. |
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引用 | ジャーナル: Acs Chem.Biol. / 年: 2012 タイトル: Structural basis of functional group activation by sulfotransferases in complex metabolic pathways. 著者: McCarthy, J.G. / Eisman, E.B. / Kulkarni, S. / Gerwick, L. / Gerwick, W.H. / Wipf, P. / Sherman, D.H. / Smith, J.L. |
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履歴 | 登録 | 2012年8月20日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2012年10月17日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2013年1月2日 | Group: Database references |
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改定 1.2 | 2017年11月15日 | Group: Refinement description / カテゴリ: software / Item: _software.name |
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改定 1.3 | 2018年1月24日 | Group: Structure summary / カテゴリ: audit_author / Item: _audit_author.name |
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改定 1.4 | 2024年2月28日 | Group: Data collection / Database references / Derived calculations カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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