ID   MEND_PROM3              Reviewed;         582 AA.
AC   A2CAW2;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   25-MAY-2022, entry version 78.
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=P9303_18801;
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABM78622.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000554; ABM78622.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A2CAW2; -.
DR   SMR; A2CAW2; -.
DR   STRING; 59922.P9303_18801; -.
DR   EnsemblBacteria; ABM78622; ABM78622; P9303_18801.
DR   KEGG; pmf:P9303_18801; -.
DR   HOGENOM; CLU_006051_4_0_3; -.
DR   UniPathway; UPA00995; -.
DR   UniPathway; UPA01057; UER00164.
DR   Proteomes; UP000002274; 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   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR42916; PTHR42916; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 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..582
FT                   /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT                   carboxylate synthase"
FT                   /id="PRO_0000341802"
SQ   SEQUENCE   582 AA;  63295 MW;  808A6C03071EBCE5 CRC64;
     MGLRHLVLCP GSRSGPLALA AGGMARTNLL RLSTAIDERS AAFLALGFST ATGTAAAVVT
     TSGTAVANLL PAAVEADRSC QPLLLLTADR PYRLKDCGAN QTVNQETFLS PACRWIGQGP
     REGLHLFSTE TLESFAEEAW QRAHHPAGAV HLNLPFEEPL HLSEEEQRVI WKGWSPKIPR
     SAPITPTNLA MAAEGTEGVT DRAPFALDPF RPGVVIAGAW RGLSKDLFAF QQSLREWQAL
     SGWPVLADPL SALPSDQPGL IRSWELLLAA GLLGSHEQLQ VLRLGPMSAS RSLEAWLKSF
     GDGQLLITEG DSRCLDPLGL SVQWSHGLTT WWQHHHHRWI DADAASQQAT QPLLKKWQII
     DRFAQDWLDQ QLPLQGAITE PALARWLSRL LPAELSIMLA ASSPVRDWLA YADKSLFSRR
     CFSFRGASGI DGTLSLSMGL AMALGPTLLV SGDLALLHDS NGWLLAHPQR PPLVVVLIDN
     GGGGIFEQLL VKKAPSEAFE QLFAMPQAVD PLVLAAAHNI PHRQVACLED LPAALEWGLF
     QTGPVLIRVC THRGQDSSMR QQLREGLVMH LQSISQNGHI DL