ID A0A7S8CC88_9BACI Unreviewed; 566 AA.
AC A0A7S8CC88;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 02-APR-2025, entry version 12.
DE RecName: Full=2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase {ECO:0000256|HAMAP-Rule:MF_01659};
DE Short=SEPHCHC synthase {ECO:0000256|HAMAP-Rule:MF_01659};
DE EC=2.2.1.9 {ECO:0000256|HAMAP-Rule:MF_01659};
DE AltName: Full=Menaquinone biosynthesis protein MenD {ECO:0000256|HAMAP-Rule:MF_01659};
GN Name=menD {ECO:0000256|HAMAP-Rule:MF_01659,
GN ECO:0000313|EMBL:QPC47319.1};
GN ORFNames=G8O30_10225 {ECO:0000313|EMBL:QPC47319.1};
OS Mangrovibacillus cuniculi.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Mangrovibacillus.
OX NCBI_TaxID=2593652 {ECO:0000313|EMBL:QPC47319.1, ECO:0000313|Proteomes:UP000593626};
RN [1] {ECO:0000313|EMBL:QPC47319.1, ECO:0000313|Proteomes:UP000593626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1DC41 {ECO:0000313|EMBL:QPC47319.1,
RC ECO:0000313|Proteomes:UP000593626};
RA Sefrji F., Michoud G., Merlino G., Daffonchio D.;
RT "Genome sequence of 2 isolates from Red Sea Mangroves.";
RL Submitted (JUL-2019) 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:0000256|HAMAP-Rule:MF_01659}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=isochorismate + 2-oxoglutarate + H(+) = 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:0000256|HAMAP-Rule:MF_01659};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01659};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01659};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01659};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01659}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01659}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01659}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. MenD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01659}.
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DR EMBL; CP049742; QPC47319.1; -; Genomic_DNA.
DR RefSeq; WP_239671990.1; NZ_CP049742.1.
DR AlphaFoldDB; A0A7S8CC88; -.
DR KEGG; mcui:G8O30_10225; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00164.
DR Proteomes; UP000593626; 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 CDD; cd07037; TPP_PYR_MenD; 1.
DR CDD; cd02009; TPP_SHCHC_synthase; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
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 InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR00173; menD; 1.
DR PANTHER; PTHR42916; 2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR42916:SF1; PROTEIN PHYLLO, CHLOROPLASTIC; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01659};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01659};
KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01659};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01659}; Reference proteome {ECO:0000313|Proteomes:UP000593626};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01659};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01659}.
FT DOMAIN 11..123
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 215..389
FT /note="Menaquinone biosynthesis protein MenD middle"
FT /evidence="ECO:0000259|Pfam:PF16582"
FT DOMAIN 424..524
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 566 AA; 63289 MW; 66DAFDAAFADBBCB3 CRC64;
MKNPILTTYV ESFTNGLIQA GLTDIVVSPG SRSTPLAYWF AEHPKLKIHI QVDERSAGFF
ALGLAKTKGR AVALLCTSGT AAANYFPAIV EANISRVPLV VLTADRPHEL RDVGAPQSIQ
QVNLFGNHVK WATDLPIADG REETNNIALF TASRAMNTSQ VSPAGAVHVN IPFREPLIPD
LEYVTNNIPI VRDFADTSIQ LTSLDQSLQE ALEDNSKGIF VCGEKNYSDA EIELLLACAE
KFHFAIVADP LSNLRFVKCL KPYIVDRYDW FLRDGRSLEH LQVDCIIRFG AMPVSKVLTQ
FIQKSTAMYI TVDEGQEYRD PTLSTSFVHA SMESFLKELL KLEGKANESN PWLIWNEVIH
SDIPNEEWSE RKIYTFLNET LPNASHVFVG NSMPIREVDL FFSKNGSEKL VFANRGANGI
DGVVSSAVGM ATCVNPSYLL IGDLSFYHDM NGLLYAKQQQ TPLTIIVINN DGGGIFSYLP
QGKMEQHYET LFGTPTGIKF KHTAAMYGIP YVKVENYQEL EKEIVPIDGP KIVEIVVDRE
NHVAQHRELW KYVSREIDYL LSDDEC
//
