ID D7GCL9_PROFC Unreviewed; 551 AA. AC D7GCL9; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 22-FEB-2023, entry version 74. 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:CBL56280.1}; GN OrderedLocusNames=PFREUD_07490 {ECO:0000313|EMBL:CBL56280.1}; OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM OS 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1). OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Propionibacterium. OX NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL56280.1, ECO:0000313|Proteomes:UP000000936}; RN [1] {ECO:0000313|EMBL:CBL56280.1, ECO:0000313|Proteomes:UP000000936} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1 RC {ECO:0000313|Proteomes:UP000000936}; RX PubMed=20668525; DOI=10.1371/journal.pone.0011748; RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S., RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P., RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C., RA Lortal S.; RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy RT actinobacterium with food and probiotic applications."; RL PLoS ONE 5:E11748-E11748(2010). 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; FN806773; CBL56280.1; -; Genomic_DNA. DR AlphaFoldDB; D7GCL9; -. DR STRING; 754252.PFREUD_07490; -. DR EnsemblBacteria; CBL56280; CBL56280; PFREUD_07490. DR KEGG; pfr:PFREUD_07490; -. DR eggNOG; COG1165; Bacteria. DR HOGENOM; CLU_006051_4_0_11; -. DR OMA; FCNRGTS; -. DR BioCyc; PFRE754252:PFREUD_RS03680-MON; -. DR UniPathway; UPA00079; -. DR UniPathway; UPA01057; UER00164. DR Proteomes; UP000000936; 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:0016829; F:lyase activity; IEA:UniProtKB-KW. 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; 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; 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 PANTHER; PTHR42916:SF1; PROTEIN PHYLLO, CHLOROPLASTIC; 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 Lyase {ECO:0000313|EMBL:CBL56280.1}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000936}; KW Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01659}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01659}. FT DOMAIN 37..208 FT /note="Thiamine pyrophosphate enzyme N-terminal TPP- FT binding" FT /evidence="ECO:0000259|Pfam:PF02776" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 216..241 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 218..236 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 551 AA; 56476 MW; 31772F627611F442 CRC64; MSNTADPQNP PQARSGEPAA AVGQAVPGGP PVRSAALARA LVTALVAHGL RDVVYCPGSR DAPFAYALDA AQHAGWLRVA VRLDERAAGF QALGLAKAAA AQGTARPVAV VTTSGTAVAN LHPAVLEADA AGVALVVVSA DRPHEMWRTG ANQTTEQLGI FAHAVRQEAD IPAGFPVDGR LSGLVRRAMT AALGNLNGNS GPVHLNVCLR EPLKPDDQWL PGPAPAPEPH REAPGAPTEL PMPDRTVVVA GDGAGDQAQQ AATAGGWPLL AEPSSGARFG ANALTDYQQL LGSPLAPQIE GVLVFGHPTL SRPVSALLAR DDVRMVAVTC GSRWTDVAGL AQVVRGPVHI ANNPQGEWLA RWIGADEPAP RSTKDTAARL IWQAHGAPDA PALVLGASAV IRSFDRRAVP GDHAPLVIAN RGLAGIDGTV STAIGVAAGT GRPVRAVVGD LTLAHDGLGL LRGMNEAVPD VQVVVLADRG GAIFAGLEHG SAAPALLSRY FLTPQVLDVR QLAGAVGASY RHVTDVLELP QVLSEPISGA SIVEVELPPV G //