(data stored in ACNUC1104 zone)

SWISSPROT: MEND_NOCSJ

ID   MEND_NOCSJ              Reviewed;         537 AA.
AC   A1SE17;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 79.
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=Noca_0510;
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the thiamine diphosphate-dependent
CC       decarboxylation of 2-oxoglutarate and the subsequent addition of
CC       the resulting succinic semialdehyde-thiamine pyrophosphate anion
CC       to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-
CC       cyclohexene-1-carboxylate (SEPHCHC). {ECO:0000255|HAMAP-
CC       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;
CC         EC=2.2.1.9; 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.
CC       {ECO:0000255|HAMAP-Rule:MF_01659};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step
CC       2/7. {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}.
DR   EMBL; CP000509; ABL80052.1; -; Genomic_DNA.
DR   RefSeq; WP_011754002.1; NC_008699.1.
DR   SMR; A1SE17; -.
DR   STRING; 196162.Noca_0510; -.
DR   PRIDE; A1SE17; -.
DR   EnsemblBacteria; ABL80052; ABL80052; Noca_0510.
DR   KEGG; nca:Noca_0510; -.
DR   eggNOG; ENOG4105C4A; Bacteria.
DR   eggNOG; COG1165; LUCA.
DR   HOGENOM; HOG000218359; -.
DR   KO; K02551; -.
DR   OMA; AIFDMLP; -.
DR   OrthoDB; 897995at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
DR   Proteomes; UP000000640; 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; 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; 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;
DR   PRODOM; A1SE17.
DR   SWISS-2DPAGE; A1SE17.
KW   Complete proteome; Magnesium; Manganese; Menaquinone biosynthesis;
KW   Metal-binding; Reference proteome; Thiamine pyrophosphate;
KW   Transferase.
FT   CHAIN         1    537       2-succinyl-5-enolpyruvyl-6-hydroxy-3-
FT                                cyclohexene-1-carboxylate synthase.
FT                                /FTId=PRO_0000341791.
SQ   SEQUENCE   537 AA;  56034 MW;  C22AECCB6674FCB4 CRC64;
     MTAPEPAPES ATATARRILA ALVEAGVTEI VVAPGSRNAP LSFAAYDAAA AGLVRLHTRL
     DERTAGFLAL GLTRSGRRAA VVCTSGTAVA NLHPAVLEAA HAGVDLVVVS ADRPARLRGT
     GANQTTDQVG IFGPLVPTQD ASGPVELLTA GPVHLNVPLE EPLVPDDRWL PDVVPGEPAH
     RVIPASLTVL ARGPRTVVVA GDDAGPRVRV LAEQAGWPLL AEPSSGSRTG DNAIRTYRLL
     LDGDLGARVE RVVVGGHPTL SRPVSRLLAR PDVEVVDLGA WGVWSERPFP VHSRILGGVG
     VDAPVDAADG TADDTDWLEE WRTADRAVSA RLDALLAAEP GLTPHEVAGA VARALPAGGL
     LVVGASSPIR DLDLMVPRYD VGARRKVVAN RGLAGIDGTI STAVGAALGR PRSTRALTLM
     GDVTFLHDAG ALVIGPGEAV PDLTIVVVND DGGSIFAMLE QGAAEYADQY DRLFGTPHRV
     DLASLCAATR TPHWRVDSLA ELEHALASPA GGIEVVEAVV RRDNRRDLDE RIRALRP
//

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