ID A0A6H2BU37_DOLFA Unreviewed; 321 AA. AC A0A6H2BU37; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 13-SEP-2023, entry version 10. DE RecName: Full=o-succinylbenzoate synthase {ECO:0000256|HAMAP-Rule:MF_00470}; DE Short=OSB synthase {ECO:0000256|HAMAP-Rule:MF_00470}; DE Short=OSBS {ECO:0000256|HAMAP-Rule:MF_00470}; DE EC=4.2.1.113 {ECO:0000256|HAMAP-Rule:MF_00470}; DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00470}; DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000256|HAMAP-Rule:MF_00470}; GN Name=menC {ECO:0000256|HAMAP-Rule:MF_00470}; GN ORFNames=HGD76_01475 {ECO:0000313|EMBL:QJB43102.1}; OS Dolichospermum flos-aquae CCAP 1403/13F. OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae; OC Dolichospermum. OX NCBI_TaxID=315271 {ECO:0000313|EMBL:QJB43102.1, ECO:0000313|Proteomes:UP000502433}; RN [1] {ECO:0000313|EMBL:QJB43102.1, ECO:0000313|Proteomes:UP000502433} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCAP 1403/13f {ECO:0000313|EMBL:QJB43102.1, RC ECO:0000313|Proteomes:UP000502433}; RA Wu V.; RT "Genome-Wide Identification of 5-Methylcytosine Sites in Bacterial Genomes RT By High-Throughput Sequencing of MspJI Restriction Fragments."; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QJB43102.1, ECO:0000313|Proteomes:UP000502433} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCAP 1403/13f {ECO:0000313|EMBL:QJB43102.1, RC ECO:0000313|Proteomes:UP000502433}; RA Fomenkov A., Anton B.P., Roberts R.J.; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1- CC carboxylate (SHCHC) to 2-succinylbenzoate (OSB). {ECO:0000256|HAMAP- CC Rule:MF_00470}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate CC = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:18325, ChEBI:CHEBI:58689; EC=4.2.1.113; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00470}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00470}; CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00470}. CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7. CC {ECO:0000256|HAMAP-Rule:MF_00470}. CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing CC enzyme family. MenC type 1 subfamily. {ECO:0000256|HAMAP- CC Rule:MF_00470}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP051206; QJB43102.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6H2BU37; -. DR KEGG; dfs:HGD76_01475; -. DR UniPathway; UPA00995; -. DR UniPathway; UPA01057; UER00165. DR Proteomes; UP000502433; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0043748; F:O-succinylbenzoate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:InterPro. DR GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd03320; OSBS; 1. DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1. DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1. DR HAMAP; MF_00470; MenC_1; 1. DR InterPro; IPR036849; Enolase-like_C_sf. DR InterPro; IPR029017; Enolase-like_N. DR InterPro; IPR029065; Enolase_C-like. DR InterPro; IPR013342; Mandelate_racemase_C. DR InterPro; IPR010196; OSB_synthase_MenC1. DR NCBIfam; TIGR01927; menC_gam_Gplu; 1. DR PANTHER; PTHR48073:SF2; O-SUCCINYLBENZOATE SYNTHASE; 1. DR PANTHER; PTHR48073; O-SUCCINYLBENZOATE SYNTHASE-RELATED; 1. DR Pfam; PF13378; MR_MLE_C; 1. DR SFLD; SFLDG00180; muconate_cycloisomerase; 1. DR SFLD; SFLDF00009; o-succinylbenzoate_synthase; 1. DR SMART; SM00922; MR_MLE; 1. DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1. DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1. PE 3: Inferred from homology; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00470}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00470}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00470}. FT DOMAIN 121..220 FT /note="Mandelate racemase/muconate lactonizing enzyme C- FT terminal" FT /evidence="ECO:0000259|SMART:SM00922" FT ACT_SITE 142 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470" FT ACT_SITE 248 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470" FT BINDING 171 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470" FT BINDING 199 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470" FT BINDING 224 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470" SQ SEQUENCE 321 AA; 36954 MW; DB92DB46E6CBE215 CRC64; MVYQFSFRYF SQKFTNPIIT NYGVWEIRES IIIRLIDEKD DVSWGEISPI SWFGSETIKQ ALDFCDQLPQ TITKEIIFAI PDKLPACQFA FESSTHPGGF RLCSSDLQSP NLTYSGLLPA GKSALNQWSN LWEQGYKTFK WKIAVDDINQ ELEIFDLLIS SLPISAKLRL DANGGLTYQE AELWLQKCDQ FLPKIEFIEQ PLAVDKFREM QELSNSYFTT IALDESIANL HQLELYFQKG WRGIFVIKPG IFGSPFRLKE FCKKRQIDVV FSSVFETEIG RQAALQLAAE LSSNNRAVGF GINHFFQPQE SNWLESLWKT C //