ID A0A2P8VJD8_9ENTR Unreviewed; 556 AA.
AC A0A2P8VJD8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=C7G83_11000 {ECO:0000313|EMBL:PSN07646.1};
OS Siccibacter turicensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Siccibacter.
OX NCBI_TaxID=357233 {ECO:0000313|EMBL:PSN07646.1, ECO:0000313|Proteomes:UP000240212};
RN [1] {ECO:0000313|EMBL:PSN07646.1, ECO:0000313|Proteomes:UP000240212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6100069499-17 {ECO:0000313|EMBL:PSN07646.1,
RC ECO:0000313|Proteomes:UP000240212};
RA Lepuschitz S., Pekard-Amenitsch S., Haunold R., Schill S., Mach R.,
RA Allerberger F., Ruppitsch W., Forsythe S.J.;
RT "Draft genome sequence of the first documented clinical Siccibacter
RT turicensis isolate in Austria.";
RL Submitted (MAR-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSN07646.1}.
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DR EMBL; PYEP01000004; PSN07646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8VJD8; -.
DR STRING; 1388748.GCA_000463155_02126; -.
DR OrthoDB; 9791859at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00164.
DR Proteomes; UP000240212; Unassembled WGS sequence.
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}; Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01659};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01659}.
FT DOMAIN 11..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 184..388
FT /note="Menaquinone biosynthesis protein MenD middle"
FT /evidence="ECO:0000259|Pfam:PF16582"
FT DOMAIN 422..534
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 556 AA; 59366 MW; C297124A5056A382 CRC64;
MSICAFNRRW ATAILEAVTR HGVQHVCIAP GSRSTPLTLA AAAHPGLTHH THFDERGLGH
LALGLAKASG QPVAVIVTSG TAVANLYPAV IEAGLTGEKL ILLTADRPPE MIDCGANQAI
RQTDIFATHP AAALSLPRPT PDIPVSWLLS AIDNLLNTHS GGAVHINCPF AEPLYGDMDA
TGEAWLQAAG SWWQERTPWL RAGQPSGVSV EPDWPAWREK RGVVIAGRLS VDEGQQVADW
AQTLGWPLIG DALSQTGQPL PCADLWLSHP QAQRELAGVE IVVQFGSSLT GKRLLQWQAS
CTPQAYWLID SLPGRLDPGH HRGRRLVASV SAWLGAHPAT VRSPWAPRLA LLAGEAQHRV
EAATSAFGEA QIAHRLPGLL PKQGQLFLGN SLVVRLIDAL AQLPAGYPVY SNRGASGIDG
LISTAAGVQR ATGRATLAII GDLSALYDLN ALALLREVSA PFVLLIINNN GGQIFSLLPT
DSTVRERFYC MPQHVEFRHA AALFGLGYQQ PADLAALRTA LDEAWQTPRA TIIEAVVSET
GGVDTLRQLL AEVSQL
//
