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MEND_THEFY
ID   MEND_THEFY              Reviewed;         553 AA.
AC   Q47Q20;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 112.
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=Tfu_1411;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/jb.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(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: 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; CP000088; AAZ55449.1; -; Genomic_DNA.
DR   RefSeq; WP_011291845.1; NC_007333.1.
DR   AlphaFoldDB; Q47Q20; -.
DR   SMR; Q47Q20; -.
DR   STRING; 269800.Tfu_1411; -.
DR   EnsemblBacteria; AAZ55449; AAZ55449; Tfu_1411.
DR   KEGG; tfu:Tfu_1411; -.
DR   eggNOG; COG1165; Bacteria.
DR   HOGENOM; CLU_006051_3_0_11; -.
DR   OMA; FCNRGTS; -.
DR   OrthoDB; 897995at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
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   PANTHER; PTHR42916; PTHR42916; 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..553
FT                   /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT                   carboxylate synthase"
FT                   /id="PRO_0000341880"
SQ   SEQUENCE   553 AA;  58246 MW;  EDC30104F4104E5C CRC64;
     MNPSTALARV LVDELARLGL TEAVIAPGSR STPLALALVA DTRIRTHVRI DERSASFLAV
     GLARASRRPV ALVCTSGTAA ANFHPAVLEA DQSGVSLIVL TADRPPELRG TGANQTVNQI
     GLYGSAVRFF AEVGVPEREA GMVAYWRSLV CRAWAAAQAN KPGPVHLNLA FREPLVPEPG
     GQPWPEPVTG RPDGKPWITV DLQRNEPEPV ELPWVERGVI VCGDGDYDPI PLLALSAQTG
     WPLLAEPTSN ARRAEALSSY RQLLAVPEFV AAHEPELVVS VGRPGLSRQL LAYLRRAPRH
     VVVGDPVAFA DPVRTATDVV GAVTAPPSAT PDTAWAASWA AAEAAARAAA DRLLDSDETL
     SELRLARDLA AHLPAGSLLF AGASMPIRDL DAVMRPRCGL RLIGNRGVSG IDGTVSTAVG
     AALAHQADGG GEAFALLGDL ALLHDQNGLL LGPDEPRPNL TIVVVNNDGG GIFSELEQAG
     HPDFERVFGT PHGVAVEQVA ATAGLPYTRV EWATDLPKAL IGDGLRLVEV RTDRAASARL
     RRALQEAVAA AVR
 
 
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