MENC_THEVB
ID MENC_THEVB Reviewed; 322 AA.
AC Q8DJP8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, 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:24872444};
DE Short=OSB synthase {ECO:0000255|HAMAP-Rule:MF_00470};
DE Short=OSBS {ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000303|PubMed:24872444};
DE EC=4.2.1.113 {ECO:0000255|HAMAP-Rule:MF_00470, 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=tlr1174 {ECO:0000312|EMBL:BAC08726.1};
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2] {ECO:0007744|PDB:2OZT, ECO:0007744|PDB:3H7V}
RP X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 2-322 OF APOENZYME AND IN COMPLEX
RP WITH MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
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).
CC -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:24872444). Does
CC not show N-succinylamino acid racemase (NSAR) activity with N-succinyl-
CC L-phenylglycine as substrate (PubMed:24872444).
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: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:24872444};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=78 uM for SHCHC {ECO:0000269|PubMed:24872444};
CC Note=kcat is 80 sec(-1) with SHCHC as substrate.
CC {ECO:0000269|PubMed:24872444};
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: Cofactor biosynthesis; phylloquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00470}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24872444}.
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; BA000039; BAC08726.1; -; Genomic_DNA.
DR RefSeq; NP_681964.1; NC_004113.1.
DR RefSeq; WP_011057016.1; NC_004113.1.
DR PDB; 2OZT; X-ray; 1.42 A; A=2-322.
DR PDB; 3H7V; X-ray; 1.70 A; A=2-322.
DR PDBsum; 2OZT; -.
DR PDBsum; 3H7V; -.
DR SMR; Q8DJP8; -.
DR STRING; 197221.22294898; -.
DR EnsemblBacteria; BAC08726; BAC08726; BAC08726.
DR KEGG; tel:tlr1174; -.
DR PATRIC; fig|197221.4.peg.1234; -.
DR eggNOG; COG4948; Bacteria.
DR OMA; TFKWKIG; -.
DR OrthoDB; 951991at2; -.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER00165.
DR EvolutionaryTrace; Q8DJP8; -.
DR Proteomes; UP000000440; Chromosome.
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:0009234; P:menaquinone biosynthetic process; IEA:InterPro.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_00470; MenC_1; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR010196; OSB_synthase_MenC1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..322
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_0000455095"
FT ACT_SITE 136
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT ACT_SITE 243
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470,
FT ECO:0000269|PubMed:24872444, ECO:0007744|PDB:3H7V"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470,
FT ECO:0000269|PubMed:24872444, ECO:0007744|PDB:3H7V"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470,
FT ECO:0000269|PubMed:24872444, ECO:0007744|PDB:3H7V"
FT STRAND 2..18
FT /evidence="ECO:0007829|PDB:2OZT"
FT STRAND 21..34
FT /evidence="ECO:0007829|PDB:2OZT"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:2OZT"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:2OZT"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:2OZT"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:2OZT"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:2OZT"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2OZT"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:2OZT"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:2OZT"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:2OZT"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:2OZT"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 250..258
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:2OZT"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:2OZT"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:2OZT"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:2OZT"
SQ SEQUENCE 322 AA; 36232 MW; E4B405306C135C77 CRC64;
MRWQWRIYEE PLQEPLTTAQ GVWRSRSGIY LRLEDEQGQV GYGEIAPLPG WGSETLNADI
ALCQQLPGHL TPEIMATIPE ALPAAQFGFA TAWQSVGRLP YRVRPWPICA LLGSGQAALE
QWQQSWQRGQ TTFKWKVGVM SPEEEQAILK ALLAALPPGA KLRLDANGSW DRATANRWFA
WLDRHGNGKI EYVEQPLPPD QWQALLSLAQ TVTTAIALDE SVVSAAEVQR WVDRGWPGFF
VIKTALFGDP DSLSLLLRRG LEPQRLVFSS ALEGAIARTA IFHLLETWQP CHALGFGVDR
WRSAPLLTTL TAYERLWERL DQ
