ID   MEND_STAA3              Reviewed;         557 AA.
AC   Q2FI34;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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};
GN   OrderedLocusNames=SAUSA300_0946;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
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; CP000255; ABD22875.1; -; Genomic_DNA.
DR   RefSeq; WP_000526687.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FI34; -.
DR   SMR; Q2FI34; -.
DR   PRIDE; Q2FI34; -.
DR   EnsemblBacteria; ABD22875; ABD22875; SAUSA300_0946.
DR   KEGG; saa:SAUSA300_0946; -.
DR   HOGENOM; CLU_006051_3_0_9; -.
DR   OMA; FCNRGTS; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
DR   Proteomes; UP000001939; 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..557
FT                   /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT                   carboxylate synthase"
FT                   /id="PRO_0000341862"
SQ   SEQUENCE   557 AA;  63078 MW;  C99072666F0769EC CRC64;
     MGNHKAALTK QVFTFASELY AYGVREVVIS PGSRSTPLAL AFEAHPNIKT WIHPDERSAA
     FFAVGLIKGS ERPVAILCTS GTAAANYTPA IAESQISRIP LIVLTSDRPH ELRSVGAPQA
     INQVNMFNNY VSYEFDMPIA DDSKETIDAI YYQMQIASQY LYGPHKGPIH FNLPFRDPLT
     PDLNATELLT SEMKILPHYQ KSIDASALRH ILNKKKGLII VGDMQHQEVD QILTYSTIYD
     LPILADPLSH LRKFDHPNVI CTYDLLFRSG LDLNVDFVIR VGKPVISKKL NQWLKKTDAF
     QILVQNNDKI DVFPIAPDIS YEISANDFFR SLMEDTTVNR VSWLEKWQCL EKKGRKEIKC
     YLEQATDESA FVGELIKKTS EKDALFISNS MPIRDVDNLL LNKNIDVYAN RGANGIDGIV
     STALGMAVHK RITLLIGDLS FYHDMNGLLM SKLNNIQMNI VLLNNDGGGI FSYLPQKESA
     TDYFERLFGT PTGLDFEYTA KLYQFDFKRF NSVSEFKNAT LLSETSTIYE LITNREDNFK
     QHQILYQKLS EMIHDTL