ID MENC_HAEIN Reviewed; 329 AA. AC P44961; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2001, sequence version 2. DT 24-JAN-2024, entry version 134. DE RecName: Full=o-succinylbenzoate synthase {ECO:0000255|HAMAP-Rule:MF_00470}; DE Short=OSB synthase {ECO:0000255|HAMAP-Rule:MF_00470}; DE Short=OSBS {ECO:0000255|HAMAP-Rule:MF_00470}; DE EC=4.2.1.113 {ECO:0000255|HAMAP-Rule:MF_00470}; DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00470}; DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000255|HAMAP-Rule:MF_00470}; GN Name=menC {ECO:0000255|HAMAP-Rule:MF_00470}; GN OrderedLocusNames=HI_0969; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1- CC carboxylate (SHCHC) to 2-succinylbenzoate (OSB). {ECO:0000255|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:0000255|HAMAP-Rule:MF_00470}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00470}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00470}. CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing CC enzyme family. MenC type 1 subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00470}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22626.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; L42023; AAC22626.1; ALT_INIT; Genomic_DNA. DR PIR; C64105; C64105. DR RefSeq; NP_439130.2; NC_000907.1. DR AlphaFoldDB; P44961; -. DR SMR; P44961; -. DR STRING; 71421.HI_0969; -. DR EnsemblBacteria; AAC22626; AAC22626; HI_0969. DR KEGG; hin:HI_0969; -. DR PATRIC; fig|71421.8.peg.1010; -. DR eggNOG; COG1441; Bacteria. DR HOGENOM; CLU_030273_0_1_6; -. DR OrthoDB; 3725747at2; -. DR PhylomeDB; P44961; -. DR UniPathway; UPA00079; -. DR UniPathway; UPA01057; UER00165. DR Proteomes; UP000000579; 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: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; IPR048639; MenC_N. 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; PF21508; MenC_N; 1. DR Pfam; PF13378; MR_MLE_C; 1. DR SFLD; SFLDS00001; Enolase; 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; Magnesium; Menaquinone biosynthesis; Metal-binding; KW Reference proteome. FT CHAIN 1..329 FT /note="o-succinylbenzoate synthase" FT /id="PRO_0000171272" FT ACT_SITE 140 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470" FT ACT_SITE 242 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470" FT BINDING 168 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470" FT BINDING 197 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470" FT BINDING 220 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470" SQ SEQUENCE 329 AA; 36970 MW; 26353A1B50D5FF60 CRC64; MAEKSFNLYR YSIPVDSQLI LRDRFLKRRE GLIVRVSCSR DGWGEIAPLP GFSEETLDQA QEQAIEWLTT WCNASCDAPR VPLDGTYPSV AFGISCAMDE MKGYLQAEGN YHTAPLCYGD PDELYAKLAS MEGEKVAKMK VGIYEANRDG LIADMFLEAI PDLQLRLDAN RHWSLEKALQ FAAKVKLQHR KRIQFLEEPC KTQALSREFA VQTDIAIAWD ESVREPNFCL EKEPHLSAVV IKPTLIGSIQ RCTELINQAH SLGLKAVISS SIESSLGLSQ LARIAQQYTP NVTPGLDTLD LMEYQVLRAW PSSDLPIVDL ESEFITKII //