ID   MEND_KLEP3              Reviewed;         556 AA.
AC   B5XNX0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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};
DE   AltName: Full=Menaquinone biosynthesis protein MenD {ECO:0000255|HAMAP-Rule:MF_01659};
GN   Name=menD {ECO:0000255|HAMAP-Rule:MF_01659}; OrderedLocusNames=KPK_1487;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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: Quinol/quinone metabolism; menaquinone 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; CP000964; ACI10445.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XNX0; -.
DR   SMR; B5XNX0; -.
DR   EnsemblBacteria; ACI10445; ACI10445; KPK_1487.
DR   KEGG; kpe:KPK_1487; -.
DR   HOGENOM; CLU_006051_3_0_6; -.
DR   OMA; FCNRGTS; -.
DR   OrthoDB; 897995at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
DR   Proteomes; UP000001734; 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   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; Menaquinone biosynthesis; Metal-binding;
KW   Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..556
FT                   /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT                   carboxylate synthase"
FT                   /id="PRO_1000187079"
SQ   SEQUENCE   556 AA;  60911 MW;  05F2F38D7D1516D2 CRC64;
     MSVSAFNRRW AAVILEALTR HGVQHICIAP GSRSTPLTLA AAENRAFIHH THFDERGLGH
     LALGLAKASR QPVAVIVTSG TATANLYPAL IEAGLTGEKL ILLTADRPPE LIDCGANQAI
     RQPGMFASHP SQTISLPRPS QDIPARWLVS TIDQALGALH AGGVHINCPF AEPLYGDMDE
     TGVEWQQQLG NWWQSDKPWL RQALQLESEK QRDWFFWRQK RGVVVAGRMS AAEGKKVAEW
     AQTLGWPLIG DVLSQTGQPL QCADLWLGNG KAVSELAQAQ IVVQLGSSLT GKRILQWQAT
     CEPDEYWLVD NLPGRLDPAQ HRGRRLLASV ERWLELHPAE KRQPWATVIP ELSRQAWQAA
     VASNEPFGEA QLAQRIRRYL PEQGQLFVGN SLVVRLIDAL AQLPAGYPVY SNRGASGIDG
     LIATAAGVQR ASARPTLAIV GDLSALYDLN SLALLRQASA PLVLIVVNNN GGQIFSMLPT
     PQDERRQFYL MPQDVDFSHA AAMFGLAYHR PDDWQSLDEA LAGAWRRAGA TVIELAVNET
     DGTQTLQQLL AQVSRL