ID MEND_PHOLL Reviewed; 564 AA. AC Q7N2K3; DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase {ECO:0000255|HAMAP-Rule:MF_01659}; DE Short=SEPHCHC synthase {ECO:0000255|HAMAP-Rule:MF_01659}; DE EC=2.2.1.9 {ECO:0000255|HAMAP-Rule:MF_01659}; DE AltName: Full=Menaquinone biosynthesis protein MenD {ECO:0000255|HAMAP-Rule:MF_01659}; GN Name=menD {ECO:0000255|HAMAP-Rule:MF_01659}; GN OrderedLocusNames=plu3073; OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / OS TT01) (Photorhabdus luminescens subsp. laumondii). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Photorhabdus. OX NCBI_TaxID=243265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15139 / CIP 105565 / TT01; RX PubMed=14528314; DOI=10.1038/nbt886; RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M., RA Glaser P., Boemare N., Danchin A., Kunst F.; RT "The genome sequence of the entomopathogenic bacterium Photorhabdus RT luminescens."; RL Nat. Biotechnol. 21:1307-1313(2003). CC -!- FUNCTION: Catalyzes the thiamine diphosphate-dependent decarboxylation CC of 2-oxoglutarate and the subsequent addition of the resulting succinic CC semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2- CC succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). CC {ECO:0000255|HAMAP-Rule:MF_01659}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6- CC hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2; CC Xref=Rhea:RHEA:25593, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29780, ChEBI:CHEBI:58818; EC=2.2.1.9; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01659}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01659}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01659}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01659}; CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01659}; CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7. CC {ECO:0000255|HAMAP-Rule:MF_01659}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01659}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01659}. CC -!- SIMILARITY: Belongs to the TPP enzyme family. MenD subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01659}. 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; BX571869; CAE15447.1; -; Genomic_DNA. DR RefSeq; WP_011147290.1; NC_005126.1. DR AlphaFoldDB; Q7N2K3; -. DR SMR; Q7N2K3; -. DR STRING; 243265.plu3073; -. DR GeneID; 24170108; -. DR KEGG; plu:plu3073; -. DR eggNOG; COG1165; Bacteria. DR HOGENOM; CLU_006051_3_0_6; -. DR OrthoDB; 9791859at2; -. DR UniPathway; UPA00079; -. DR UniPathway; UPA01057; UER00164. DR Proteomes; UP000002514; Chromosome. DR GO; GO:0070204; F:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd07037; TPP_PYR_MenD; 1. DR CDD; cd02009; TPP_SHCHC_synthase; 1. DR Gene3D; 3.40.50.970; -; 2. DR Gene3D; 3.40.50.1220; TPP-binding domain; 1. DR HAMAP; MF_01659; MenD; 1. DR InterPro; IPR004433; MenaQ_synth_MenD. DR InterPro; IPR032264; MenD_middle. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR InterPro; IPR011766; TPP_enzyme_TPP-bd. DR NCBIfam; TIGR00173; menD; 1. DR PANTHER; PTHR42916; 2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE-1-CARBOXYLATE SYNTHASE; 1. DR PANTHER; PTHR42916:SF1; PROTEIN PHYLLO, CHLOROPLASTIC; 1. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF16582; TPP_enzyme_M_2; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR PIRSF; PIRSF004983; MenD; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2. PE 3: Inferred from homology; KW Magnesium; Manganese; Menaquinone biosynthesis; Metal-binding; KW Reference proteome; Thiamine pyrophosphate; Transferase. FT CHAIN 1..564 FT /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1- FT carboxylate synthase" FT /id="PRO_0000341796" SQ SEQUENCE 564 AA; 62123 MW; 114D626C10D4EDAE CRC64; MSNSAFNRRW AELLLEALTR HGLRHVCIAP GSRSTPLTIA AAANNKLICH THFDERGLGH LALGLSKASR EPVAVIVTSG TAVANLYPSL IEASLTGERM VFLTADRPPE LMDCGANQAI RQNGIFASHP CQTISLPRPT VDIPASWLAS VIDHSMANLQ HGAVHINCPF AEPLYGNEEP AYDEWQQQLG DWWKSKTPWL SQPVAKVVAE VPDWDCWQQK KGVVLAGRMS AEEGVNVAKW AKALSWPLIG NALSQTGQPL PCADLWLDNP HVQEILAQAQ LVVQFGSSLI GKCLLQWQAK CQPQEFWIID PIPGRLDPAN HRGKKLTCHI ADWLLAHPAQ PCIPWAQSCT LWAEELIVWS EKAVNCVRTE LAGKFGEATV AYRLRELLPE RGQLFVGNSL IIRLIDTLGQ LPAGYPVYSN RGASGIDGLI STAAGVQRAT AKPTLAVIGD LSALYDLNSL ALLRHPSAPM VLIVVNNNGG QIFSLLPTQE EARQRFYCMP QYVNFDHAAA MFGLKYASPQ NWMELQQSIK QAWQQNETTL IELKVPDREG AECLQQLLKQ VAML //