ID   MEND_PROM5              Reviewed;         588 AA.
AC   A2BVS0;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=P9515_06721;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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}.
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DR   EMBL; CP000552; ABM71881.1; -; Genomic_DNA.
DR   RefSeq; WP_011819986.1; NC_008817.1.
DR   AlphaFoldDB; A2BVS0; -.
DR   SMR; A2BVS0; -.
DR   STRING; 167542.P9515_06721; -.
DR   EnsemblBacteria; ABM71881; ABM71881; P9515_06721.
DR   KEGG; pmc:P9515_06721; -.
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; UP000001589; 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; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   PANTHER; PTHR42916; PTHR42916; 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..588
FT                   /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT                   carboxylate synthase"
FT                   /id="PRO_0000341805"
SQ   SEQUENCE   588 AA;  65896 MW;  84BBE7C57F04526A CRC64;
     MTSSIECQNI FRSLQLLDLF IKIGVKNLIL CPGSRSAPLA IAAGELYKYG ILNVFNSIDE
     RSAGFHSLGI STASGDISLV VTTSGSAVGN LLPAAVEADR SCKSIVFITA DRPLRLKNCG
     SNQTVNQEAF LNSVCRSTLS TNLNGIHKNN DDDILKIVKM IKKQLLQSPG PIHLNIPFEK
     PLDISLKNKR KTLKVFETLY LNKTCKFLKQ NEQNKSIHFS KRIFESLDLS NSGIIIVGPY
     QGSIKDLVSF NNSLEKIQSI TGWPVFADPV SGVSADLRGL VENWELIIKK NNNVIKCNQI
     LRLGPLSSSN NLEKFLSDFD GIQILVKENN RRKLDPIKKS LEYEFGLTNF VNQLLGTYSD
     DQKKKKPLIN LVKVLRREGQ KISKILNEQI FLNKEITEYK LANFVPKIWP ENYPIMLSAS
     SPIRDWLTFS ENGTLTRKCF SFRGASGIDG TLSLALGIAR ITQPLLLVTG DLALIHDING
     FLIENSIDLN LTVLLINNNG GNIFNNLYKN NLEKEELKKL FLMPKSINWE NLAKAFQVPI
     KIVSDLNKLP ESFEWSLSMQ KSVIIKVDIN VDNEMKERSL ILKKILNN