MEND_DESPS
ID MEND_DESPS Reviewed; 537 AA.
AC Q6ARP3;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=DP0253;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(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;
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; CR522870; CAG34982.1; -; Genomic_DNA.
DR RefSeq; WP_011187498.1; NC_006138.1.
DR AlphaFoldDB; Q6ARP3; -.
DR SMR; Q6ARP3; -.
DR STRING; 177439.DP0253; -.
DR EnsemblBacteria; CAG34982; CAG34982; DP0253.
DR KEGG; dps:DP0253; -.
DR eggNOG; COG1165; Bacteria.
DR HOGENOM; CLU_006051_3_0_7; -.
DR OMA; PAAWIGQ; -.
DR OrthoDB; 897995at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00164.
DR Proteomes; UP000000602; 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; IPR029035; DHS-like_NAD/FAD-binding_dom.
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; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00173; menD; 1.
PE 3: Inferred from homology;
KW Magnesium; Manganese; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..537
FT /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT carboxylate synthase"
FT /id="PRO_0000341733"
SQ SEQUENCE 537 AA; 58155 MW; E7F739E86347F749 CRC64;
MRAKQHISDL AHHCIAHGMR HLVISPGSRN APLIRAFAAS SQIECLSIVD ERSAAFVALG
LATELQAPVG VLCTSGTALL NYGPAIAEAY YLRAPLIVLS ADRPARLVGQ QDSQTICQDN
LFANIVKGSY SLPEEPETVA ELELSARVIA QAFSTALSPC FGPVHINIPL DEPLYGGELM
AESLIALSPL QLAEPKGMSP ALWQEVESAW RGAKRRMIVC GQGVADAELQ ALLARFAPDK
TVTIIAENTA NIVGPWLVDR PDAVLLACDE ASRSLLAPDC LISFGGHLVA KHIKLLLREF
KPAFHFRLDP AQMGIDTYQC LSAELDLAPT TFFRRLAQQV EPAAGFRDLW ALPEGVAENQ
DDEFLVLKRL LGQLPAGSIA HLGNSMSVRH AQKLASRADL LYHSNRGVAG IDGCLSTAVG
VALATDQLVL CCLGDLSFVY DSNALWNRNL PSNLRIVILN NQGGDIFRRL KGPSVSPGYQ
DFFVAHHPVQ IGKMIEAYGV AYRRCLASEI DGFSEEFLGL QDGPLVLEVF VDPTKRD
