ID A0A857ZA07_9BACT Unreviewed; 536 AA. AC A0A857ZA07; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 14-DEC-2022, entry version 4. DE RecName: Full=2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase {ECO:0000256|HAMAP-Rule:MF_01659}; DE Short=SEPHCHC synthase {ECO:0000256|HAMAP-Rule:MF_01659}; DE EC=2.2.1.9 {ECO:0000256|HAMAP-Rule:MF_01659}; DE AltName: Full=Menaquinone biosynthesis protein MenD {ECO:0000256|HAMAP-Rule:MF_01659}; GN Name=menD {ECO:0000256|HAMAP-Rule:MF_01659, GN ECO:0000313|EMBL:QHV69048.1}; GN ORFNames=DMI79_12330 {ECO:0000313|EMBL:QHV69048.1}; OS Akkermansia muciniphila. OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Akkermansiaceae; Akkermansia. OX NCBI_TaxID=239935 {ECO:0000313|EMBL:QHV69048.1, ECO:0000313|Proteomes:UP000630024}; RN [1] {ECO:0000313|EMBL:QHV69048.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=EB-AMDK-47 {ECO:0000313|EMBL:QHV69048.1}; RA Nam Y.-D., Chung W.-H., Park Y.S., Kang J.; RT "Complete genome sequnece of Akkermansia muciniphila EB-AMDK-47."; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|HAMAP-Rule:MF_01659}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01659}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01659}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01659}; CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01659}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_01659}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01659}. CC -!- SIMILARITY: Belongs to the TPP enzyme family. MenD subfamily. CC {ECO:0000256|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; CP029704; QHV69048.1; -; Genomic_DNA. DR UniPathway; UPA00079; -. DR UniPathway; UPA01057; UER00164. DR Proteomes; UP000630024; 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 HAMAP; MF_01659; MenD; 1. DR InterPro; IPR004433; MenaQ_synth_MenD. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR PANTHER; PTHR42916; 2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE-1-CARBOXYLATE SYNTHASE; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR PIRSF; PIRSF004983; MenD; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2. DR TIGRFAMs; TIGR00173; menD; 1. PE 3: Inferred from homology; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01659}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01659}; KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01659}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01659}; Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01659}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01659}. FT DOMAIN 25..152 FT /note="TPP_enzyme_N" FT /evidence="ECO:0000259|Pfam:PF02776" SQ SEQUENCE 536 AA; 58144 MW; 786F33F33085C49B CRC64; MIPVNSSASF VKSLLAQCCL GGICEWVVCP GARNMALLQV LAAAEDLVKW THFDERSAAF FALGRIQDMG LPVAVVTTSG TAAAELLPAV VEAYYQRRPL LLLTADRPAA CRGSAAPQAI EQADLFGIYA PTIDLETPES LPEDILQDWD YASPLHINVC LPDPDPAWNP GSCDLYPAEP PEENGFRGSL AELARALRFK SRDGLVVMIG GLDPTEQAPA RWLANELKAP VVADATSGLR EELAHLALTD ADALLREHPP AVLLRLGDVP VGRFWRDLED IPATEVFSVT RTGFSGLARP SSVVTGDLEA ILHALGDIDT VGDVNGLRTM NKRRKALMEE LLITCPESEQ AMVRSFSCFA ADGDCIYLGN SMPVRYWNSF AQTSIPTENV RANRGANGID GQISGFLGVS ARCSRSWALV GDLTAMYDSN ALALLPQLDR GTRVLGVINN GGGGIFRTLP GADGQPETMR KLLVQPHAHS FKAIAEQWGM RYLTIRTAED FDQLDSLEEN SQTLVELIPD REQTEQIRLR LANAQV //