MEND_LISMF
ID MEND_LISMF Reviewed; 580 AA.
AC Q71YZ2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=LMOf2365_1699;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(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; AE017262; AAT04472.1; -; Genomic_DNA.
DR RefSeq; WP_010958930.1; NC_002973.6.
DR PDB; 3LQ1; X-ray; 2.60 A; A/B=2-568.
DR PDBsum; 3LQ1; -.
DR AlphaFoldDB; Q71YZ2; -.
DR SMR; Q71YZ2; -.
DR KEGG; lmf:LMOf2365_1699; -.
DR HOGENOM; CLU_006051_3_0_9; -.
DR OMA; FCNRGTS; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00164.
DR EvolutionaryTrace; Q71YZ2; -.
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 1: Evidence at protein level;
KW 3D-structure; Magnesium; Manganese; Menaquinone biosynthesis;
KW Metal-binding; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..580
FT /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT carboxylate synthase"
FT /id="PRO_0000341769"
FT HELIX 4..21
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:3LQ1"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:3LQ1"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 144..162
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:3LQ1"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 357..377
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 388..396
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 399..405
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 409..417
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 422..428
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 439..446
FT /evidence="ECO:0007829|PDB:3LQ1"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 450..458
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 459..464
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 466..469
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 470..474
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 479..484
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 517..522
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:3LQ1"
FT HELIX 533..543
FT /evidence="ECO:0007829|PDB:3LQ1"
FT STRAND 546..554
FT /evidence="ECO:0007829|PDB:3LQ1"
SQ SEQUENCE 580 AA; 64580 MW; 768C95F532F0EFAB CRC64;
MTNHEQVLTD YLAAFIEELV QAGVKEAIIS PGSRSTPLAL MMAEHPILKI YVDVDERSAG
FFALGLAKAS KRPVVLLCTS GTAAANYFPA VAEANLSQIP LIVLTADRPH ELRNVGAPQA
MDQLHLYGSH VKDFTDMALP ENSEEMLRYA KWHGSRAVDI AMKTPRGPVH LNFPLREPLV
PILEPSPFTA TGKKHHHVHI YYTHEVLDDS SIQKMVTECT GKKGVFVVGP IDKKELEQPM
VDLAKKLGWP ILADPLSGLR SYGALDEVVI DQYDAFLKEA EIIDKLTPEV VIRFGSMPVS
KPLKNWLEQL SDIRFYVVDP GAAWKDPIKA VTDMIHCDER FLLDIMQQNM PDDAKDAAWL
NGWTSYNKVA REIVLAEMAN TTILEEGKIV AELRRLLPDK AGLFIGNSMP IRDVDTYFSQ
IDKKIKMLAN RGANGIDGVV SSALGASVVF QPMFLLIGDL SFYHDMNGLL MAKKYKMNLT
IVIVNNDGGG IFSFLPQANE PKYFESLFGT STELDFRFAA AFYDADYHEA KSVDELEEAI
DKASYHKGLD IIEVKTNRHE NKANHQALWV KIADALKALD
