MEND_PROM9
ID MEND_PROM9 Reviewed; 587 AA.
AC Q31BS7;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
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};
GN Name=menD {ECO:0000255|HAMAP-Rule:MF_01659};
GN OrderedLocusNames=PMT9312_0607;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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: Cofactor biosynthesis; phylloquinone 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; CP000111; ABB49668.1; -; Genomic_DNA.
DR RefSeq; WP_011376163.1; NC_007577.1.
DR AlphaFoldDB; Q31BS7; -.
DR SMR; Q31BS7; -.
DR STRING; 74546.PMT9312_0607; -.
DR EnsemblBacteria; ABB49668; ABB49668; PMT9312_0607.
DR KEGG; pmi:PMT9312_0607; -.
DR eggNOG; COG1165; Bacteria.
DR HOGENOM; CLU_006051_3_0_3; -.
DR OMA; FCNRGTS; -.
DR OrthoDB; 897995at2; -.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER00164.
DR Proteomes; UP000002715; 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:InterPro.
DR GO; GO:0042372; P:phylloquinone 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;
KW Magnesium; Manganese; Metal-binding; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..587
FT /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT carboxylate synthase"
FT /id="PRO_0000341803"
SQ SEQUENCE 587 AA; 65733 MW; 57B1B607D3642669 CRC64;
MTSSIECKNF LRSLQLLNLL IKIGVQNLIV CPGSRSAPLA IAAGELNKLG LVNIFNSIDE
RSAGFHSLGI SAASGNLSLV ITTSGTAVSN LLPAAVEADR SCKGIIFLTA DRPLRLKDCG
ANQTVNQEDF LSSVCRRVLS TNLNGLHETQ ENEILNLVQI TEKQISTFPG PIHLNIPIDK
PLGISFLNKK NVLEVFERIY LKKKYVFQEV EIKSNKNKFL EILENLNLDE SGIILVGPYQ
GSINELSSFN KSLEKLQAIT GWPVFADPVS CVYSDLRGLV VNWELVLRKN KNLINCHQLL
RLGPMSSSID LEDFLTTFEG IQILIKEKNY RKLDPIKKSF EYDFGLLNFI TLLLAELSIN
KINTKSLTPL AIDLMEEGEQ IKKILKEKIT NDNQITEYKL ANLVPKLWPA ENPIMLSASS
PIRDWLTFSE NGTLTRNCFS FRGASGIDGT LSLALGISRI KNPLLLVTGD LAFVHDLNGW
LIENSIDLNL TILLINNNGG NIFNRLYKDN LKEDELKKLF LMPKEINWKK LAEGYQVNFK
SVTNFKKLRE AFEWSISIRE SVIIKVDIDP ENEISDKNAL LEKIIGS
