ID A0A265N958_9BACI Unreviewed; 579 AA.
AC A0A265N958;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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=CIL03_09565 {ECO:0000313|EMBL:OZU88542.1};
OS Virgibacillus indicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=2024554 {ECO:0000313|EMBL:OZU88542.1, ECO:0000313|Proteomes:UP000216498};
RN [1] {ECO:0000313|EMBL:OZU88542.1, ECO:0000313|Proteomes:UP000216498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IO3-P2-C2 {ECO:0000313|EMBL:OZU88542.1,
RC ECO:0000313|Proteomes:UP000216498};
RA Xu B., Hu B., Wang J., Zhu Y., Huang L., Du W., Huang Y.;
RT "Virgibacillus indicus sp. nov. and Virgibacillus profoundi sp. nov, two
RT moderately halophilic bacteria isolated from marine sediment by using the
RT Microfluidic Streak Plate.";
RL Submitted (AUG-2017) 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:OZU88542.1}.
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DR EMBL; NPMS01000004; OZU88542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A265N958; -.
DR OrthoDB; 9791859at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00164.
DR Proteomes; UP000216498; 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; IPR029035; DHS-like_NAD/FAD-binding_dom.
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; SSF52467; DHS-like NAD/FAD-binding domain; 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:UP000216498};
KW Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01659};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01659}.
FT DOMAIN 14..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 206..402
FT /note="Menaquinone biosynthesis protein MenD middle"
FT /evidence="ECO:0000259|Pfam:PF16582"
FT DOMAIN 438..552
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 579 AA; 64705 MW; 444CD5877B99D167 CRC64;
MNHTETLTRY TANFVDELSI NGLTDVVISP GSRSTPLALT FSEHKQIKEW IIIDERSAAF
FALGMAKQTK RPVALVCTSG TAAANYFPAI VEAHYSRVPL IVLTADRPHE LRDVGAPQAI
EQLKLYGDYV KWFQEMAVPE ATPAMLRFVR SKAARSVYMA QEGNAGPVHL NFPFREPLNP
DFSLENIWGV EYEQSYMPAL DGKKRLEQNQ LEQLIEKLKE KQNGIIVCGP QTDEIFAKAV
TNLAAQWELP VLADPLSQVR SGQHHKDNVI ETYDAILRNE EIREKLKPDF IIRFGAMPVS
KPYLFYVKEH IQAMQLVVES HTGYREPAGN ATEFIFADPV LLCEDLIQTE TALNFDTGWL
DEWKRMNLIA KKHLLNGTEE KITEGEAVRG LMEVIPDSSS LYTGNSMAVR DVDTFFMTTP
KNISVLANRG ANGIDGMVSS GMGAAASGDP VTLLLGDLSF FHDMNGLLAA KHYNLNITIL
IVNNNGGGIF SFLPQANDQK HFEALFGTPA DVDFKHGIMM YGGEYSLVST EEELKEALFT
SYQNKGLSVV EVKTDRVTNA QWHRHKWKQI ETEILGDGN
//
