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Entry: E8NG50_MICTS
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ID   E8NG50_MICTS            Unreviewed;       597 AA.
AC   E8NG50;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 76.
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   OrderedLocusNames=MTES_2349 {ECO:0000313|EMBL:BAJ75313.1};
OS   Microbacterium testaceum (strain StLB037).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ75313.1, ECO:0000313|Proteomes:UP000008975};
RN   [1] {ECO:0000313|EMBL:BAJ75313.1, ECO:0000313|Proteomes:UP000008975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB037 {ECO:0000313|EMBL:BAJ75313.1,
RC   ECO:0000313|Proteomes:UP000008975};
RX   PubMed=21357489; DOI=10.1128/JB.00180-11;
RA   Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT   lactone-degrading bacterium isolated from potato leaves.";
RL   J. Bacteriol. 193:2072-2073(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=StLB037;
RA   Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AP012052; BAJ75313.1; -; Genomic_DNA.
DR   RefSeq; WP_013585438.1; NC_015125.1.
DR   AlphaFoldDB; E8NG50; -.
DR   STRING; 979556.MTES_2349; -.
DR   KEGG; mts:MTES_2349; -.
DR   eggNOG; COG1165; Bacteria.
DR   HOGENOM; CLU_006051_4_0_11; -.
DR   OMA; FCNRGTS; -.
DR   OrthoDB; 9791859at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
DR   Proteomes; UP000008975; 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:UniProtKB-UniRule.
DR   CDD; cd07037; TPP_PYR_MenD; 1.
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   NCBIfam; TIGR00173; menD; 1.
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.
PE   3: Inferred from homology;
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|HAMAP-Rule:MF_01659};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01659};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01659}.
FT   DOMAIN          15..127
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
SQ   SEQUENCE   597 AA;  61718 MW;  0E4D1A6C35C9DC9C CRC64;
     MSTTAERAAA PSTDAAAALL AGLVARGVRH LVISPGSRSQ ALALVAADLE RAGLVHLHVR
     IDERVAGFTA LGIGRETGMP AVVVCTSGTA VANLLPAALE AHHAGVPLLL LTADRPPELR
     GVGANQTTRQ PGLFRAAARF EADLPVPDAV DHDGTAEQTA EFDTVAATAL AAALGEGARA
     AGPVHLNVPL REPLAGAVPG WLLERATARP VAAASDIESD PEAEASGALY QGGGGIGVAD
     VAPETEAAFP LELGARTIVV AGADAGPAAE ELAHRGGFPL VAEIVSGARF GRNVVHGYRA
     LLRDPDLGGR IERVVVLGHP TLSREVALLL GRDDVEVIAV RGPGEPVNLN GTTQGVDAVR
     VTSGETDRAW LGEWMRASRA AAVDLSPPAP DADGLASAVP HERLGAINAE VEVIRAPLDR
     AALVDALWRA TWPHDRLMFG SSRLVRVADE LLSGKKVSVH ANRGLAGIDG TIATATGIAL
     ASQVEERPGV TRVLLGDLAF LHDLGALLLP PGEDEPRLQV VVGNDGGGTI FDGLEVASVA
     GDDAMDRVQY TPHTTRLEPL ALAFGWEYHR VTTRVALDQV LTAPGGGRQL IEVPLPR
//
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