MEND_GEOKA
ID MEND_GEOKA Reviewed; 577 AA.
AC Q5KVX6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase {ECO:0000255|HAMAP-Rule:MF_01659};
DE Short=SEPHCHC synthase {ECO:0000255|HAMAP-Rule:MF_01659};
DE EC=2.2.1.9 {ECO:0000255|HAMAP-Rule:MF_01659};
DE AltName: Full=Menaquinone biosynthesis protein MenD {ECO:0000255|HAMAP-Rule:MF_01659};
GN Name=menD {ECO:0000255|HAMAP-Rule:MF_01659}; OrderedLocusNames=GK2875;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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:0000255|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:0000255|HAMAP-Rule:MF_01659};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01659}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01659}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01659}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. MenD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01659}.
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DR EMBL; BA000043; BAD77160.1; -; Genomic_DNA.
DR RefSeq; WP_011232347.1; NC_006510.1.
DR AlphaFoldDB; Q5KVX6; -.
DR SMR; Q5KVX6; -.
DR STRING; 235909.GK2875; -.
DR EnsemblBacteria; BAD77160; BAD77160; GK2875.
DR KEGG; gka:GK2875; -.
DR PATRIC; fig|235909.7.peg.3069; -.
DR eggNOG; COG1165; Bacteria.
DR HOGENOM; CLU_006051_3_0_9; -.
DR OMA; FCNRGTS; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00164.
DR Proteomes; UP000001172; 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 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-bd_C.
DR PANTHER; PTHR42916; PTHR42916; 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; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00173; menD; 1.
PE 3: Inferred from homology;
KW Magnesium; Manganese; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..577
FT /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT carboxylate synthase"
FT /id="PRO_0000341749"
SQ SEQUENCE 577 AA; 62975 MW; 6D108994DC292549 CRC64;
MADALSVYAA ALVDGLAQAG VTEAVISPGS RSTPLAMAMA AHPGLRLYMN IDERSAAFFA
LGLAKAKQRP VALVCTSGTA AANYGPAVVE AYYSRVPLVV LTADRPHELR DVGAPQAIDQ
LHLYGRYAKW FVDLALPEEA DDMLRYARTM AARAVQTAAG APCGPVHVNA PFREPLVPHI
DEAVWERVRS VSRAPQVWRG RPALPQESVS ALYEQLSAAE RGLIVCGPLD RPGFAEAVTE
LARALDFPIL ADPLSQLRAG THDKTYVLDS YDAILREETA ASKLVPDVVL RFGAMPVSKP
LFLWLKRHRA IRQIVVDDGG WRDPTLSADS FVQSDEWILC RQLLEWAKPK ENKSAWSAIW
REMNAIARAA LERHLPKEEW FEGNVFTELA DLLPAGAALF VGNSMPIRDA DTFLFATDKP
LRVLANRGAN GIDGVVSSAL GASVAANPLV LVIGDLSFYH DLNGLLAAKM HSLSATIVLL
NNNGGGIFSF LPQARHKGAF ETLFGTPTDL SFAHAVEMYG GRHTVPHNWA EFRRHVSESL
SSGGLHVIEV RTSRAENVRM HRLLWNEVAR EIAKCLE
