AC MF_01934; DC Protein; auto TR HAMAP; MF_01934; -; 1; level=0 XX Names: MenB XX ID MENB DE RecName: Full=1,4-dihydroxy-2-naphthoyl-CoA synthase; DE Short=DHNA-CoA synthase; DE EC=4.1.3.36; GN Name=menB; XX CC -!- FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2- CC naphthoyl-CoA (DHNA-CoA). CC -!- CATALYTIC ACTIVITY: CC Reaction=2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA + CC H2O; Xref=Rhea:RHEA:26562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57364, ChEBI:CHEBI:58897; EC=4.1.3.36; case CC -!- COFACTOR: CC Name=hydrogencarbonate; Xref=ChEBI:CHEBI:17544; end case CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7. case not CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. else case CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis. end case CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. MenB CC subfamily. XX DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1; trigger=no DR Pfam; PF00378; ECH; 1; trigger=no DR NCBIfam; TIGR01929; menB; 1; trigger=no XX KW Lyase case not KW Menaquinone biosynthesis end case XX GO GO:0008935; F:1,4-dihydroxy-2-naphthoyl-CoA synthase activity case not GO GO:0009234; P:menaquinone biosynthetic process else case GO GO:0042372; P:phylloquinone biosynthetic process end case XX FT From: MENB_ECOLI (P0ABU0) FT BINDING 84..88 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT Optional; Condition: [SAVT]-G-G-[DN]-Q FT BINDING 129..133 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT BINDING 154..156 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT Tag: hydrogencarbonate; Optional; Condition: Q-T-G FT BINDING 45 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT Optional; Condition: R FT BINDING 97 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT Optional; Condition: Y FT BINDING 155 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT Optional; Condition: T FT BINDING 161 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT Optional; Condition: S FT BINDING 258 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT Optional; Condition: Y FT BINDING 273 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT Optional; Condition: K FT SITE 97 FT /note="Important for catalysis" FT Condition: Y FT SITE 258 FT /note="Important for catalysis" FT Condition: Y FT From: MENB_MYCTU (P9WNP5) FT SITE 185 FT /note="Important for catalysis" FT Optional; Condition: D XX Size: 250-391; Related: None; Template: P0ABU0; P23966; A0QRD3; P9WNP5; Q7CQ56; Q5HH38; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: The hydrogencarbonate anion plays the same catalytic role (proton acceptor) as the side-chain carboxylate group of the essential 'Asp-185' found in actinobacteria, archaea, bacteroidetes, and deltaproteobacteria. XX # Revision 1.13 2023/06/01 //