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Database: UniProt
Entry: A0A0D5M0B1_9GAMM
LinkDB: A0A0D5M0B1_9GAMM
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ID   A0A0D5M0B1_9GAMM        Unreviewed;       580 AA.
AC   A0A0D5M0B1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=KO116_00674 {ECO:0000313|EMBL:AJY49173.1};
OS   Halomonas sp. KO116.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY49173.1, ECO:0000313|Proteomes:UP000028645};
RN   [1] {ECO:0000313|EMBL:AJY49173.1, ECO:0000313|Proteomes:UP000028645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KO116 {ECO:0000313|EMBL:AJY49173.1,
RC   ECO:0000313|Proteomes:UP000028645};
RX   PubMed=25953187;
RA   O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT   "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT   Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL   Genome Announc. 3:0-0(2015).
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; CP011052; AJY49173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D5M0B1; -.
DR   STRING; 1504981.KO116_00674; -.
DR   KEGG; hak:KO116_00674; -.
DR   eggNOG; COG1165; Bacteria.
DR   HOGENOM; CLU_006051_3_0_6; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
DR   Proteomes; UP000028645; 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:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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}; Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01659};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01659}.
FT   DOMAIN          23..136
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          199..406
FT                   /note="Menaquinone biosynthesis protein MenD middle"
FT                   /evidence="ECO:0000259|Pfam:PF16582"
FT   DOMAIN          423..555
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   580 AA;  64040 MW;  30F6A0245871BB3A CRC64;
     MHMTAPTSSG FAKAHATFNH VWAALMLEEL YRLGVRDIAL APGSRSSPLT MVASEHAGLR
     CHCHFDERGL GFMALGIARG SQRPVVIITT SGTAVANLYP AVVEANLLGV PLIVLSADRP
     IELLDNGSNQ AIDQRDIFSR YTIVHHDLPP PDAEIKASFL LSTLDQAVDQ QRRTPGPIHI
     NCRYREPLYP GNCLVDASDY LAPLRDWLTT VKPWSDWSSS TAVPALNHAW ETFAQQRGLI
     VVGSVDDHKQ AQQIVELSKQ LGWPLLADIQ SQIHFDPHNL VHFDLALHDE RFSAELAKAE
     VLLQFGGRLI SKRLTQFIAQ KPWQDVWLVD PLSQRLDPDY CVKRRLVGSP ADFIAALPTI
     SEQLSWHQLT SLQRRTSRLV EERCKTFSEV SICHHLAQLA EGQLFIGNSL PARLMNMLGT
     DRRTPLQVFA NRGASGIDGL IATAYGVSFT HLGPTTIVLG DTSALHDLNS LALLKQAVQP
     LVVVILNNDG GSIFHLLPVP KEGELLERYY RQPHGLSFEY AAKMFGLGYS APYSLDAFSA
     AYTQALQAGV TLIEIKVPHQ QVADDLIALG VMLREEQGEQ
//
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