ID   MEND_NOCFA              Reviewed;         545 AA.
AC   Q5YPA6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=NFA_51330;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01659};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-
CC         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; AP006618; BAD59985.1; -; Genomic_DNA.
DR   RefSeq; WP_011211667.1; NC_006361.1.
DR   AlphaFoldDB; Q5YPA6; -.
DR   SMR; Q5YPA6; -.
DR   STRING; 247156.NFA_51330; -.
DR   GeneID; 61135711; -.
DR   KEGG; nfa:NFA_51330; -.
DR   eggNOG; COG1165; Bacteria.
DR   HOGENOM; CLU_006051_4_0_11; -.
DR   OrthoDB; 9791859at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
DR   Proteomes; UP000006820; 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   InterPro; IPR011766; TPP_enzyme_TPP-bd.
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; PF02775; TPP_enzyme_C; 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; Manganese; Menaquinone biosynthesis; Metal-binding;
KW   Reference proteome; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..545
FT                   /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT                   carboxylate synthase"
FT                   /id="PRO_0000341790"
SQ   SEQUENCE   545 AA;  56577 MW;  FB1DA1B4E63A4696 CRC64;
     MNPSTAQARV VVDELVRGGV RDVVLCPGSR NAPLAFALQA ADAAGRLRLH MRIDERTAGF
     LAIGLAISAG APVPVVMTSG TAVANLGPAV LEANYARVPL IVLSANRPYE MLGTGANQTV
     EQLGLFGSQV RATISLGLAE ADGAGAGSYD QQNSVWRSAV CRVLAAARGT RSGNAGPVHF
     DIPLREPLVP DLAEGEAEPA GRAGGAPWTA TQYATLDVPL EIDLTPDTVV VSGHGAGLRP
     ELAHLPTVAE PTAPMHGPAL HPLALPLLTP RQAIITGRPT LHRQVSRLLA DPAVTVYALT
     TGPRWPDVSG NVVGTGTRAV TSGGPRPEWL AHCRELDEKA RQVVRAELAG HPKPTGLHVA
     AVVMDALREG DQLLLGASNP VRDAALVATP RPGVRVLSNR GVAGIDGTVS TAVGAALAHP
     GRTIALIGDL TFLHDAAGLL IGRGEPRPAD LTIVVANDDG GGIFELLEQG DPQYAGVFER
     VFGTPHGMDL AALCAAYRIP HRQVDPAELA AELAGDAHGL RVLEVITERS SLRELHATVR
     AKIAP
//