ID A0A1M6N047_9FLAO Unreviewed; 554 AA.
AC A0A1M6N047;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN04487908_13032 {ECO:0000313|EMBL:SHJ89040.1};
OS Aequorivita viscosa.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=797419 {ECO:0000313|EMBL:SHJ89040.1, ECO:0000313|Proteomes:UP000184172};
RN [1] {ECO:0000313|Proteomes:UP000184172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26349 {ECO:0000313|Proteomes:UP000184172};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FQYV01000030; SHJ89040.1; -; Genomic_DNA.
DR RefSeq; WP_073221365.1; NZ_FQYV01000030.1.
DR AlphaFoldDB; A0A1M6N047; -.
DR STRING; 797419.SAMN05216556_12832; -.
DR OrthoDB; 9791859at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00164.
DR Proteomes; UP000184172; 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}; Reference proteome {ECO:0000313|Proteomes:UP000184172};
KW Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01659};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01659}.
FT DOMAIN 9..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 208..385
FT /note="Menaquinone biosynthesis protein MenD middle"
FT /evidence="ECO:0000259|Pfam:PF16582"
FT DOMAIN 396..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 554 AA; 62439 MW; FCF015691E33FDFF CRC64;
MKFSTKILSQ TLVQLCLDKG IKHIVISPGS RNAPLTIGFG EHSEFKCFSI IDERSAAFFA
MGMAQQLKKP VAVVCTSGSA LLNYYPAIAE AFYSDIPLVI LSADRPAKFI DIGDGQTIRQ
ENVFENHILY SANCKEGSEH QLFNETEINI ALNTAFELNG PVHINIPFSE PLYITTEERL
VAPQNVLPRL SDNILNEDLS HFEDVWNRSK RKMILVGVLQ PNSLESRFVE QLAKDESVLV
LTETTSNLNH PNFIAAIDQL IAPLTDEDFK LLQPEVLLTF GGMIVSKKIK AFVRNFPPKT
HWHVDPKKAY DTFFVLEHHF KSTINNFFSE FLPKTTAVKS DYRNHWLQVK SHRLLRHQLY
ETQIPYSDFM VFCTLIKELP QNIQLQLSNS ATIRYAQLFD IPKTIEVFCN RGTSGIDGST
STAVGAAFAS KLPTVFLTGD LSFFYDSNAL WNKYIPNCFK IIVINNGGGG IFRILPGEKD
TSLFDTYFET KHNLSAKQLS EMYGFNYSAI NEGEGLQKKI AAFFNQSNGP ALLEIFTPST
VNDAVLINYF KFIS
//
