ID   MEND_SYNJA              Reviewed;         597 AA.
AC   Q2JY06;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 96.
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};
GN   Name=menD {ECO:0000255|HAMAP-Rule:MF_01659}; OrderedLocusNames=CYA_0082;
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS   A-Prime).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=321327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-3-3Ab;
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-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: Cofactor biosynthesis; phylloquinone 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; CP000239; ABC98311.1; -; Genomic_DNA.
DR   RefSeq; WP_011429003.1; NC_007775.1.
DR   AlphaFoldDB; Q2JY06; -.
DR   SMR; Q2JY06; -.
DR   STRING; 321327.CYA_0082; -.
DR   EnsemblBacteria; ABC98311; ABC98311; CYA_0082.
DR   KEGG; cya:CYA_0082; -.
DR   eggNOG; COG1165; Bacteria.
DR   HOGENOM; CLU_006051_3_0_3; -.
DR   OMA; FCNRGTS; -.
DR   OrthoDB; 897995at2; -.
DR   UniPathway; UPA00995; -.
DR   UniPathway; UPA01057; UER00164.
DR   Proteomes; UP000008818; 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:InterPro.
DR   GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniRule.
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-bd_C.
DR   PANTHER; PTHR42916; PTHR42916; 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; SSF52518; 2.
DR   TIGRFAMs; TIGR00173; menD; 1.
PE   3: Inferred from homology;
KW   Magnesium; Manganese; Metal-binding; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..597
FT                   /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT                   carboxylate synthase"
FT                   /id="PRO_0000341873"
SQ   SEQUENCE   597 AA;  65936 MW;  EAA7AF884CE72074 CRC64;
     MTGANSLQRL DWRNLNTLWG SILAETLSRL GCRVAVVCPG SRSAPLTYAL AQHPEIEAIP
     AVDERSAAFF ALGLAQQTRQ PIPLVCTSGS AGAHFFPALI EAAESGWPLL VLTADRPPEL
     RHCRAGQTID QVKLYGHYPN WQAELALPSA DLEALAYLRQ MIIHAWERAL YPFPGPVHLN
     VPLRDPLAPV ADGSTAPLVH LQEDPEFEKT FFRGVISPSG LVTPAGGSAF ASTASFWREW
     CGCERGVILA GPAQPADPQR YAEAVARLAL ALGWPVLAEG LSPLRNYASL NPYLITTYDF
     LLQGEQPPLW PEQVIQLGSL PTSKALRQTL AQARPRTWLL DPRAQNADPL HNPTTHLPFV
     VEEVAAGIPA GKAKATAFLQ TWLRAEAKAR AELDRLLADL PEWFEGKLAW WLAHHLPPET
     PLFIANSTPV RDVEWFWPPN DRRIRPYFNR GTNGIDGILS TAFGVAYRHR PTVLLTGDLA
     FLHDCGGLRL AQCLQGSLTI LLINNQGGGI FELLPIAEAG PPFEPYFATP QAVDFALLCQ
     AHGIPHRRIE TWEELAQALD PLPAQGVRVL EILTDRRADA RRRQEWFRRW SELPSTL