(data stored in ACNUC7421 zone)

SWISSPROT: MEND_SHESH

ID   MEND_SHESH              Reviewed;         569 AA.
AC   A8FPR6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 66.
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=Ssed_0226;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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: Isochorismate + 2-oxoglutarate = 5-
CC       enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate +
CC       CO(2). {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; CP000821; ABV34839.1; -; Genomic_DNA.
DR   RefSeq; WP_012004365.1; NC_009831.1.
DR   ProteinModelPortal; A8FPR6; -.
DR   SMR; A8FPR6; -.
DR   STRING; 425104.Ssed_0226; -.
DR   EnsemblBacteria; ABV34839; ABV34839; Ssed_0226.
DR   KEGG; sse:Ssed_0226; -.
DR   eggNOG; ENOG4105C4A; Bacteria.
DR   eggNOG; COG1165; LUCA.
DR   HOGENOM; HOG000218360; -.
DR   KO; K02551; -.
DR   OMA; IFRILPG; -.
DR   OrthoDB; POG091H058U; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0070204; F:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1220; -; 1.
DR   HAMAP; MF_01659; MenD; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
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;
DR   PRODOM; A8FPR6.
DR   SWISS-2DPAGE; A8FPR6.
KW   Complete proteome; Magnesium; Manganese; Menaquinone biosynthesis;
KW   Metal-binding; Thiamine pyrophosphate; Transferase.
FT   CHAIN         1    569       2-succinyl-5-enolpyruvyl-6-hydroxy-3-
FT                                cyclohexene-1-carboxylate synthase.
FT                                /FTId=PRO_0000341837.
SQ   SEQUENCE   569 AA;  62637 MW;  357C1D25210E7100 CRC64;
     MQIDKTAELN LLWGTLILEE LSRLGVQHVC MAPGSRSTPL TLAAAKQSKL KQHLHFDERG
     LGFMALGLAK TSHAPVAIIT TSGTAVANLY PAIIEAWLTQ VPLVVLSGDR PPELIDCGAN
     QAIIQPALFA QYAKQINLPT PDIAIRPEAL LTMLDEAISN QSLPVHINCM FREPLYPSTM
     SADFTQYLST LGNWQHTTSP FNQYGKTSQH SLPTQDSLAR FVHGKGVIIA GTLSPQESPE
     ILVELSQKLG WPLLTDAQSQ LRQHSGVIGN VDQLLHQPKA RALLAQAESV LVFGGRLLSK
     RLINFLSEQK WKRYWQVLPQ QMRLDPSHSA KQVWHSSVAA FASQAWPRSS DANWALQLIQ
     FNDGLETLFQ QQIDNAEFGE AMVVRAIAKA QNRQSQLFIG NSLPVRLYDM YAPITPDYPR
     TYTNRGASGI DGLLATACGV AKHEGKATTL LIGDISQLHD LNSLAIARTI ESPFVIVILN
     NDGGNIFNLL PVPDEKLRSD YYRLAHGLEF GYGAAMFGLA YNRVDDFESF NEAYQEAIAF
     QGPSVIEVSV AQHQASEQIA SIATWVKQS
//

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