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Database: UniProt
Entry: A0A126Z3X4_9MICO
LinkDB: A0A126Z3X4_9MICO
Original site: A0A126Z3X4_9MICO 
ID   A0A126Z3X4_9MICO        Unreviewed;       596 AA.
AC   A0A126Z3X4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   ORFNames=AX769_19180 {ECO:0000313|EMBL:AMM21883.1};
OS   Frondihabitans sp. PAMC 28766.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frondihabitans.
OX   NCBI_TaxID=1795630 {ECO:0000313|EMBL:AMM21883.1, ECO:0000313|Proteomes:UP000070552};
RN   [1] {ECO:0000313|EMBL:AMM21883.1, ECO:0000313|Proteomes:UP000070552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC28744 {ECO:0000313|Proteomes:UP000070552};
RA   Park H.;
RT   "Complete genome of Frondihabitans sp.";
RL   Submitted (FEB-2016) 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=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: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; CP014513; AMM21883.1; -; Genomic_DNA.
DR   RefSeq; WP_066282344.1; NZ_CP014513.1.
DR   AlphaFoldDB; A0A126Z3X4; -.
DR   STRING; 1795630.AX769_19180; -.
DR   KEGG; frp:AX769_19180; -.
DR   OrthoDB; 9791859at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
DR   Proteomes; UP000070552; 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; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
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; 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|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|HAMAP-Rule:MF_01659};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070552};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01659};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01659}.
FT   DOMAIN          18..134
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   REGION          200..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   596 AA;  62039 MW;  91DED4A75377B3FC CRC64;
     MPSTELPLPS GSPATDFAVV LLAELERAGV RDIVLSPGSR SQALALAAAE FERAGRLRLH
     VRLDERSSGF LALGLAVEQG LPAAVVTTSG TAVANLHPAV LEAHHSGVPM ILLTADRPPE
     LRGIGANQTT HQSALFGESL RLLRDVDAPG DSRVDGAVVR ELVREAMSAA LGRSSSPDEP
     ATPGPVQLNI AFREPLSAKA TSLPARADET EGAGSGGPAP WHPAASMTPP LALEVDVDPA
     TVVVAGHGAG PDAEETAHLL GAPLVAEVSS GARFGRNLAP AYRELLDAPE FGGRVRRAIV
     FGHPTLTRQV PALLKRADVE VIVVRGPVPE AYDPSHGATV VEAVQVEASE RSSDLAHREW
     VGTWVQTGRE LVGDDDEAAP DLDAATSDDP AVRAAFLRGE VDVIRRPVTR RSLVEALWRA
     TWPHDRLVLG ASRLIREADV FVPGKKIAVH ANRGLAGIDG TIATATGIGL ASQAGGVGGG
     RLGWADGARG VTRVLVGDLT LLHDAGSLLF GEGEAKPRIQ VIVGNDGGGT IFDGLEVAQV
     APADAMRRVQ STPQPISFEH LAAAYGWEYV RAATRGELEQ ALVGSPGPVL VEVPLG
//
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