ID D7GCL9_PROFC Unreviewed; 551 AA. AC D7GCL9; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 04-MAR-2015, entry version 31. DE RecName: Full=2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase {ECO:0000256|HAMAP-Rule:MF_01659, ECO:0000256|SAAS:SAAS00056887}; DE Short=SEPHCHC synthase {ECO:0000256|HAMAP-Rule:MF_01659}; DE EC=2.2.1.9 {ECO:0000256|HAMAP-Rule:MF_01659, ECO:0000256|SAAS:SAAS00056850}; 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 / OS CIP 103027 / CIRM-BIA1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; 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 / CIP 103027 / 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., RA Gaillardin C., Lortal S.; RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a RT hardy actinobacterium with food and probiotic applications."; RL PLoS ONE 5:E11748-E11748(2010). CC -!- FUNCTION: Catalyzes the thiamine diphosphate-dependent CC decarboxylation of 2-oxoglutarate and the subsequent addition of CC the resulting succinic semialdehyde-thiamine pyrophosphate anion CC to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3- CC cyclohexene-1-carboxylate (SEPHCHC). {ECO:0000256|HAMAP- CC Rule:MF_01659, ECO:0000256|SAAS:SAAS00056921}. CC -!- CATALYTIC ACTIVITY: Isochorismate + 2-oxoglutarate = 5- CC enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CC CO(2). {ECO:0000256|HAMAP-Rule:MF_01659, CC ECO:0000256|SAAS:SAAS00056925}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01659, ECO:0000256|SAAS:SAAS00169927}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01659, ECO:0000256|SAAS:SAAS00169927}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01659, CC ECO:0000256|SAAS:SAAS00169938}; CC Note=Binds 1 thiamine pyrophosphate per subunit. CC {ECO:0000256|HAMAP-Rule:MF_01659, ECO:0000256|SAAS:SAAS00169938}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Note=Binds 1 thiamine pyrophosphate per subunit.; CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step CC 2/7. {ECO:0000256|HAMAP-Rule:MF_01659, CC ECO:0000256|SAAS:SAAS00160671}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_01659}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01659, CC ECO:0000256|SAAS:SAAS00056810}. 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 RefSeq; WP_013160665.1; NC_014215.1. DR RefSeq; YP_003687720.1; NC_014215.1. DR EnsemblBacteria; CBL56280; CBL56280; PFREUD_07490. DR GeneID; 9283865; -. DR KEGG; pfr:PFREUD_07490; -. DR HOGENOM; HOG000218359; -. DR KO; K02551; -. DR BioCyc; PFRE754252:GI1A-795-MONOMER; -. 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-HAMAP. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.970; -; 2. 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 Pfam; PF02776; TPP_enzyme_N; 1. DR PIRSF; PIRSF004983; MenD; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR TIGRFAMs; TIGR00173; menD; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000936}; KW Lyase {ECO:0000313|EMBL:CBL56280.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01659, KW ECO:0000256|SAAS:SAAS00056803}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01659, KW ECO:0000256|SAAS:SAAS00056877}; KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01659}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01659, KW ECO:0000256|SAAS:SAAS00056906}; KW Reference proteome {ECO:0000313|Proteomes:UP000000936}; KW Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01659, KW ECO:0000256|SAAS:SAAS00089813}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01659, KW ECO:0000256|SAAS:SAAS00056836}. 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 //