ID A0A2D7NQR3_9DELT Unreviewed; 471 AA. AC A0A2D7NQR3; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 11-DEC-2019, entry version 8. DE RecName: Full=Isochorismate synthase MenF {ECO:0000256|HAMAP-Rule:MF_01935}; DE EC=5.4.4.2 {ECO:0000256|HAMAP-Rule:MF_01935}; DE AltName: Full=Isochorismate mutase {ECO:0000256|HAMAP-Rule:MF_01935}; GN Name=menF {ECO:0000256|HAMAP-Rule:MF_01935}; GN ORFNames=CL937_06135 {ECO:0000313|EMBL:MAJ49269.1}; OS Deltaproteobacteria bacterium. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:MAJ49269.1, ECO:0000313|Proteomes:UP000226880}; RN [1] {ECO:0000313|Proteomes:UP000226880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the RT Global Oceans."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of chorismate to isochorismate. CC {ECO:0000256|HAMAP-Rule:MF_01935}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate = isochorismate; Xref=Rhea:RHEA:18985, CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29780; EC=5.4.4.2; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01935}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01935}; CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 1/7. CC {ECO:0000256|HAMAP-Rule:MF_01935}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_01935}. CC -!- SIMILARITY: Belongs to the isochorismate synthase family. CC {ECO:0000256|HAMAP-Rule:MF_01935}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MAJ49269.1}. 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; NZHX01000088; MAJ49269.1; -; Genomic_DNA. DR UniPathway; UPA00079; -. DR UniPathway; UPA01057; UER00163. DR Proteomes; UP000226880; Unassembled WGS sequence. DR GO; GO:0008909; F:isochorismate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.60.120.10; -; 1. DR HAMAP; MF_01935; MenF; 1. DR InterPro; IPR005801; ADC_synthase. DR InterPro; IPR015890; Chorismate_C. DR InterPro; IPR004561; IsoChor_synthase. DR InterPro; IPR034681; MenF. DR Pfam; PF00425; Chorismate_bind; 1. DR SUPFAM; SSF56322; SSF56322; 1. DR TIGRFAMs; TIGR00543; isochor_syn; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01935}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01935}; KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01935}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01935}. FT DOMAIN 208..460 FT /note="Chorismate_bind" FT /evidence="ECO:0000259|Pfam:PF00425" FT COILED 166..186 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 228 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935" FT ACT_SITE 278 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935" FT METAL 322 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935" FT METAL 456 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935" SQ SEQUENCE 471 AA; 53906 MW; 6C2902CBBE40510F CRC64; MLASPQTLDP KAPSTLSKAI EDLLEQLDQL GKGKLGTSLT GEGIIRLETK ASVEDPLSWL HTQKNNKKHF WREREGGETI AGVGECLVFE SEHGSTIELM LQRIRRLLNN SSDGVRIFGG IRFNLSSDSI SDEWKSWKQA RFVIPEIELI RDGKETRLAC NLNSVVLDKN RSLEGLRRRI SELSEEDSNN ILESNFQFLK KNHKPEYENW CDNVNQALSE IKSGTLNKIV LARKTEYQLQ EAYDPLKFLL RLRDRAPNAY QYCFQFDKDQ AWMGISPERL YKRQSRKIET EAVASTRPRG TNNEEDKNLA LELLQSQKEV REHDLVLERI ESVLNQFCDK ITRKSYREIL KLRQVQHLLS RIEGHLNPDH GESTLINAIH PTPAVCGIPD EKARLNIEQL ENFDRGWYAG PVGWISKNGA EFAVGIRSAQ IHHKTLRIYT GAGIVQGSDP DSEWNEIDAK LRNWESILEP A //