MEND_NOSS1
ID MEND_NOSS1 Reviewed; 583 AA.
AC Q8YZZ2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 110.
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}; OrderedLocusNames=alr0312;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB72270.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000019; BAB72270.1; ALT_INIT; Genomic_DNA.
DR PIR; AH1845; AH1845.
DR RefSeq; WP_010994488.1; NZ_RSCN01000076.1.
DR AlphaFoldDB; Q8YZZ2; -.
DR SMR; Q8YZZ2; -.
DR STRING; 103690.17129657; -.
DR EnsemblBacteria; BAB72270; BAB72270; BAB72270.
DR KEGG; ana:alr0312; -.
DR eggNOG; COG1165; Bacteria.
DR OMA; FCNRGTS; -.
DR OrthoDB; 897995at2; -.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER00164.
DR Proteomes; UP000002483; 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; 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; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..583
FT /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT carboxylate synthase"
FT /id="PRO_0000341699"
SQ SEQUENCE 583 AA; 65729 MW; 1B790BE73D11C24D CRC64;
MPIAYKNINQ LWAYIFTETL KRLGLAYAVI CPGSRSTPLA VAFAQQAPNI EAISILDERS
AAFFALGIAK ATNRPVAIVC TSGTAGANFY PAVIEAQESR VPLLLLTADR PPELRDCHSG
QTIDQMKLYG SYPNWQAELA LPVSDMGMLA YLRQTLVHSW YRMQAPTPGP VHLNIPFRDP
LAPIPDGTDL SYLLAKFHPE EFFAGITDTT PLPHHSPLSI PPEWLQSQRG IIIAGVAQPQ
QPQEYCRAIA RLSQTLQWPV LAEGLSPVRN YADFNPYLIS TYDLILRNQQ LATRLAPDMV
IQIGDMPTSK ELRNWIDTHQ PRRWVIDPSD QNLDPLHGRT THLRIRVEEL GYQGVEEDKS
SVSEYLQLWC NAETKVRVNV DETLDKMEDL VECKAAWLLS QMLPPETPLF IANSMPVRDV
EFFWKPNNLR VRSHFNRGAN GIDGTLSTAL GISHRQQSSV LITGDLALLH DTNGFLIRNK
FVGHLTIILI NNNGGGIFEM LPIAKFEPPF EEFFGTPQDI DFAQLCTTYN VQHELIHSWV
HLQQRLNPLP NTGIRVLELR TNRKIDAQWR RDNLSNFAAD NII
