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Database: UniProt
Entry: G8X646_FLACA
LinkDB: G8X646_FLACA
Original site: G8X646_FLACA 
ID   G8X646_FLACA            Unreviewed;       554 AA.
AC   G8X646;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 64.
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   OrderedLocusNames=FCOL_07285 {ECO:0000313|EMBL:AEW86276.1};
OS   Flavobacterium columnare (strain ATCC 49512 / CIP 103533 / TG 44/87).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1041826 {ECO:0000313|EMBL:AEW86276.1, ECO:0000313|Proteomes:UP000005638};
RN   [1] {ECO:0000313|Proteomes:UP000005638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49512 / CIP 103533 / TG 44/87
RC   {ECO:0000313|Proteomes:UP000005638};
RA   Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D., Benton N.R., Zaitshik J.,
RA   Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., Waldbieser G.C.,
RA   Lawrence M.L.;
RT   "Complete genome sequence of Flavobacterium columnare ATCC 49512.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEW86276.1, ECO:0000313|Proteomes:UP000005638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49512 / CIP 103533 / TG 44/87
RC   {ECO:0000313|Proteomes:UP000005638};
RX   PubMed=22535941; DOI=10.1128/JB.00281-12;
RA   Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D.W., Benton N.R., Zaitshik J.,
RA   Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., Waldbieser G.C.,
RA   Lawrence M.L.;
RT   "Genome Sequence of the Fish Pathogen Flavobacterium columnare ATCC
RT   49512.";
RL   J. Bacteriol. 194:2763-2764(2012).
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; CP003222; AEW86276.1; -; Genomic_DNA.
DR   RefSeq; WP_014165551.1; NC_016510.2.
DR   AlphaFoldDB; G8X646; -.
DR   STRING; 1041826.FCOL_07285; -.
DR   KEGG; fco:FCOL_07285; -.
DR   eggNOG; COG1165; Bacteria.
DR   HOGENOM; CLU_006051_3_0_10; -.
DR   OMA; FCNRGTS; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
DR   Proteomes; UP000005638; 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; 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:UP000005638};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01659};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01659}.
FT   DOMAIN          12..124
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          211..386
FT                   /note="Menaquinone biosynthesis protein MenD middle"
FT                   /evidence="ECO:0000259|Pfam:PF16582"
FT   DOMAIN          396..525
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   554 AA;  63359 MW;  041DBF11B9F22615 CRC64;
     MKPTAIYPRI PLAQSIIEIC KNKGLKHIVI SPGSRNAPLT IGFSNQTEFN CYSIVDERCA
     GFFALGLAQQ LQEPVVLICT SGSALLNYYP AISEAFYSQI PLVVISADRP IDKIDIGDGQ
     TIRQANVFAN HILYNANLQE DASSENDRLI QEALFLSISQ KGPVHINAPF EEPLYETIPE
     PTIKPIWFNF QKKDEQLDAL EIFAEEWNLA QKKIILIGEN HSDSIDTKYL DIIARDPSVI
     VMTEVTSNVH HENFITNIDT IITPFSEEEF ERYKPEILLT LGGMIVSKRI KTFFRKYKPN
     THWHIDELRA YDTYGCLKKH FKVKPNVFFE HFLKLTSYKE SSFQKEVLAI RSQRAILHTL
     YLKELSFSDL KVFQIITELL PENIQLQISN SSAIRYAQLF SIDPSISVYC NRGTSGIEGS
     TTTAIGAAVA SKKTTYFITG DISFFYDSNA LWNHYIPNDF KIIIINNGGG GIFRILPGHQ
     ENETFNTFFE TSHSLTAEYL AKMYGFDYFK ATEENQLRTD WKTFSLLNKP AIYEIFTPEK
     RNNEILIQYF KELK
//
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