MENC_THEFY
ID MENC_THEFY Reviewed; 317 AA.
AC Q47Q21;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=o-succinylbenzoate synthase {ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000303|PubMed:24060347};
DE Short=OSB synthase {ECO:0000255|HAMAP-Rule:MF_00470};
DE Short=OSBS {ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000303|PubMed:24060347};
DE EC=4.2.1.113 {ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000269|PubMed:24060347, ECO:0000269|PubMed:24872444};
DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00470};
DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000255|HAMAP-Rule:MF_00470};
GN Name=menC {ECO:0000255|HAMAP-Rule:MF_00470};
GN OrderedLocusNames=Tfu_1410 {ECO:0000312|EMBL:AAZ55448.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24872444; DOI=10.1073/pnas.1318703111;
RA Odokonyero D., Sakai A., Patskovsky Y., Malashkevich V.N., Fedorov A.A.,
RA Bonanno J.B., Fedorov E.V., Toro R., Agarwal R., Wang C., Ozerova N.D.,
RA Yew W.S., Sauder J.M., Swaminathan S., Burley S.K., Almo S.C.,
RA Glasner M.E.;
RT "Loss of quaternary structure is associated with rapid sequence divergence
RT in the OSBS family.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:8535-8540(2014).
RN [3] {ECO:0007744|PDB:2OPJ, ECO:0007744|PDB:2QVH}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-317 OF APOENZYME AND IN COMPLEX
RP WITH 2-SUCCINYLBENZOIC ACID AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, AND MUTAGENESIS
RP OF PHE-14; ARG-15; PHE-37; TYR-40; ASN-71; THR-73; ARG-126; VAL-228 AND
RP GLY-252.
RC STRAIN=YX;
RX PubMed=24060347; DOI=10.1021/bi401176d;
RA Odokonyero D., Ragumani S., Lopez M.S., Bonanno J.B., Ozerova N.D.,
RA Woodard D.R., Machala B.W., Swaminathan S., Burley S.K., Almo S.C.,
RA Glasner M.E.;
RT "Divergent evolution of ligand binding in the o-succinylbenzoate synthase
RT family.";
RL Biochemistry 52:7512-7521(2013).
CC -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:24060347,
CC PubMed:24872444). Does not show N-succinylamino acid racemase (NSAR)
CC activity with N-succinyl-L-phenylglycine as substrate
CC (PubMed:24872444). {ECO:0000269|PubMed:24060347,
CC ECO:0000269|PubMed:24872444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate
CC = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18325, ChEBI:CHEBI:58689; EC=4.2.1.113;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00470,
CC ECO:0000269|PubMed:24060347, ECO:0000269|PubMed:24872444};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00470,
CC ECO:0000269|PubMed:24060347};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=182 uM for SHCHC {ECO:0000269|PubMed:24060347};
CC Note=kcat is 122 sec(-1) with SHCHC as substrate.
CC {ECO:0000269|PubMed:24060347};
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7.
CC {ECO:0000255|HAMAP-Rule:MF_00470}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00470}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24060347}.
CC -!- DOMAIN: The 20s loop, a flexible loop in the active site that permits
CC ligand binding and release in most enolase superfamily proteins, has a
CC four-amino acid deletion and is well-ordered in T.fusca OSBS.
CC {ECO:0000269|PubMed:24060347}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. MenC type 1 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00470}.
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DR EMBL; CP000088; AAZ55448.1; -; Genomic_DNA.
DR RefSeq; WP_011291844.1; NC_007333.1.
DR PDB; 2OPJ; X-ray; 1.60 A; A=2-317.
DR PDB; 2QVH; X-ray; 1.76 A; A/B=2-317.
DR PDBsum; 2OPJ; -.
DR PDBsum; 2QVH; -.
DR SMR; Q47Q21; -.
DR STRING; 269800.Tfu_1410; -.
DR DrugBank; DB02251; O-Succinylbenzoate.
DR EnsemblBacteria; AAZ55448; AAZ55448; Tfu_1410.
DR KEGG; tfu:Tfu_1410; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_057696_0_0_11; -.
DR OMA; ANAAWDV; -.
DR OrthoDB; 951991at2; -.
DR BRENDA; 4.2.1.113; 6298.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR EvolutionaryTrace; Q47Q21; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043748; F:O-succinylbenzoate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.120; -; 1.
DR HAMAP; MF_00470; MenC_1; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR010196; OSB_synthase_MenC1.
DR InterPro; IPR041338; OSBS_N.
DR Pfam; PF18374; Enolase_like_N; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Menaquinone biosynthesis; Metal-binding.
FT CHAIN 1..317
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_0000455094"
FT ACT_SITE 97
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT BINDING 71..73
FT /ligand="2-succinylbenzoate"
FT /ligand_id="ChEBI:CHEBI:18325"
FT /evidence="ECO:0000269|PubMed:24060347,
FT ECO:0007744|PDB:2QVH"
FT BINDING 95
FT /ligand="2-succinylbenzoate"
FT /ligand_id="ChEBI:CHEBI:18325"
FT /evidence="ECO:0000269|PubMed:24060347,
FT ECO:0007744|PDB:2QVH"
FT BINDING 128..130
FT /ligand="2-succinylbenzoate"
FT /ligand_id="ChEBI:CHEBI:18325"
FT /evidence="ECO:0000269|PubMed:24060347,
FT ECO:0007744|PDB:2QVH"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470,
FT ECO:0000269|PubMed:24060347, ECO:0007744|PDB:2QVH"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470,
FT ECO:0000269|PubMed:24060347, ECO:0007744|PDB:2QVH"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470,
FT ECO:0000269|PubMed:24060347, ECO:0007744|PDB:2QVH"
FT BINDING 201
FT /ligand="2-succinylbenzoate"
FT /ligand_id="ChEBI:CHEBI:18325"
FT /evidence="ECO:0000269|PubMed:24060347,
FT ECO:0007744|PDB:2QVH"
FT MUTAGEN 14
FT /note="F->A: 5.6-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:24060347"
FT MUTAGEN 15
FT /note="R->A: 7.7-fold decrease in catalytic efficiency. 71-
FT fold decrease in catalytic efficiency; when associated with
FT A-40. 166-fold decrease in catalytic efficiency; when
FT associated with A-37."
FT /evidence="ECO:0000269|PubMed:24060347"
FT MUTAGEN 37
FT /note="F->A: 2.7-fold decrease in catalytic efficiency.
FT 166-fold decrease in catalytic efficiency; when associated
FT with A-15."
FT /evidence="ECO:0000269|PubMed:24060347"
FT MUTAGEN 40
FT /note="Y->A: 2-fold decrease in catalytic efficiency. 71-
FT fold decrease in catalytic efficiency; when associated with
FT A-15."
FT /evidence="ECO:0000269|PubMed:24060347"
FT MUTAGEN 71
FT /note="N->A: 20-fold decrease in catalytic efficiency. 33-
FT fold decrease in catalytic efficiency; when associated with
FT L-73."
FT /evidence="ECO:0000269|PubMed:24060347"
FT MUTAGEN 71
FT /note="N->L: 1111-fold decrease in catalytic efficiency;
FT when associated with V-73."
FT /evidence="ECO:0000269|PubMed:24060347"
FT MUTAGEN 73
FT /note="T->A: 2-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:24060347"
FT MUTAGEN 73
FT /note="T->L: 2-fold decrease in catalytic efficiency. 33-
FT fold decrease in catalytic efficiency; when associated with
FT A-71."
FT /evidence="ECO:0000269|PubMed:24060347"
FT MUTAGEN 73
FT /note="T->V: 1111-fold decrease in catalytic efficiency;
FT when associated with L-71."
FT /evidence="ECO:0000269|PubMed:24060347"
FT MUTAGEN 126
FT /note="R->M: 3-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:24060347"
FT MUTAGEN 228
FT /note="V->L: 3.3-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:24060347"
FT MUTAGEN 252
FT /note="G->A: 3.6-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:24060347"
FT MUTAGEN 252
FT /note="G->T: 33-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:24060347"
FT STRAND 2..14
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 17..26
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 42..57
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:2QVH"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:2QVH"
FT TURN 189..193
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:2OPJ"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:2OPJ"
FT HELIX 295..309
FT /evidence="ECO:0007829|PDB:2OPJ"
SQ SEQUENCE 317 AA; 34100 MW; 6EE0C6BF295A81B0 CRC64;
MTGRAFAIPL RTRFRGITVR EGMLVRGAAG WGEFSPFAEY GPRECARWWA ACYEAAELGW
PAPVRDTVPV NATVPAVGPE EAARIVASSG CTTAKVKVAE RGQSEANDVA RVEAVRDALG
PRGRVRIDVN GAWDVDTAVR MIRLLDRFEL EYVEQPCATV DELAEVRRRV SVPIAADESI
RRAEDPLRVR DAEAADVVVL KVQPLGGVRA ALRLAEECGL PVVVSSAVET SVGLAAGVAL
AAALPELPYA CGLATLRLLH ADVCDDPLLP VHGVLPVRRV DVSEQRLAEV EIDPAAWQAR
LAAARAAWEQ VEREPGP
