MEND_HAEIG
ID MEND_HAEIG Reviewed; 568 AA.
AC A5UGA0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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};
GN OrderedLocusNames=CGSHiGG_04210;
OS Haemophilus influenzae (strain PittGG).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374931;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittGG;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
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; CP000672; ABQ99805.1; -; Genomic_DNA.
DR RefSeq; WP_012054938.1; NC_009567.1.
DR AlphaFoldDB; A5UGA0; -.
DR SMR; A5UGA0; -.
DR EnsemblBacteria; ABQ99805; ABQ99805; CGSHiGG_04210.
DR KEGG; hiq:CGSHiGG_04210; -.
DR HOGENOM; CLU_006051_3_0_6; -.
DR OMA; FCNRGTS; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00164.
DR Proteomes; UP000001990; 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; 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; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00173; menD; 1.
PE 3: Inferred from homology;
KW Magnesium; Manganese; Menaquinone biosynthesis; Metal-binding;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..568
FT /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT carboxylate synthase"
FT /id="PRO_0000341755"
SQ SEQUENCE 568 AA; 63113 MW; 8238553C1B1AFB17 CRC64;
MSVSVFNRCW SKVILETLVR QGVSHVCIAP GSRSTPLTLE AVRLQNAGSV TCHTHFDERG
LGFFALGIAK ATQSPVAIIV TSGTATANLY PAIIEARQTG VNLFVLTADR PPELWECGAN
QAILQQNMFG QYPVANVNLP KPNADYSAQW LISLLEQAAF QQKQQGGVVH INVPFAEPLY
DATDEEVNSH SWLQPLQRWL IQKKSWINVE VQQNEVLMHE NWDHWRTKRG VVVVGQLPAE
QAMGINSWAS AMGWVLLTDI QSGVVPTTPY EDIWLANQTV REKLLQADIV IQFGARFISK
RINQFLQAFK GEFWLVEQSG KALDPYHHSL TRFNAKVHHW LRAHPPLRQK PWLLEPLALS
KFCATFIEQQ VGGNLTEASL ALRLPTLLPY NGVLFLGNSL LVRLVDALTQ LPESYPVYTN
RGASGIDGLL ATAAGIGIGS NKPVVAVIGD TSTLYDLNSF ALFKNVTQPT LIFVINNNGG
AIFDMLPVDE QVKDQFYRLP HNGDFSQIAA MFDLKYAHPY TWADLNSVVK QAYSRRKATL
IEIKTNPSDG SSLYKRLIEQ ISHAVIGA
