MENC_LISIN
ID MENC_LISIN Reviewed; 374 AA.
AC Q927X3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=o-succinylbenzoate synthase {ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000303|PubMed:24872444};
DE Short=OSB synthase {ECO:0000255|HAMAP-Rule:MF_01933};
DE Short=OSBS {ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000303|PubMed:24872444};
DE EC=4.2.1.113 {ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000269|PubMed:24872444};
DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000255|HAMAP-Rule:MF_01933};
DE AltName: Full=N-succinylamino acid racemase {ECO:0000303|PubMed:24872444};
DE Short=NSAR {ECO:0000303|PubMed:24872444};
DE EC=5.1.1.- {ECO:0000269|PubMed:24872444};
DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000255|HAMAP-Rule:MF_01933};
GN Name=menC {ECO:0000255|HAMAP-Rule:MF_01933};
GN OrderedLocusNames=lin2664 {ECO:0000312|EMBL:CAC97890.1};
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2] {ECO:0007744|PDB:1WUF}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC BAA-680 / CLIP 11262;
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). Also
CC acts as a N-succinylamino acid racemase (NSAR) that catalyzes the
CC racemization of N-succinyl-L-phenylglycine (PubMed:24872444). L.innocua
CC has the menaquinone synthesis pathway, indicating that the species
CC requires OSBS activity. However, the NSAR/OSBS is not encoded in the
CC menaquinone operon, raising the possibility that both NSAR and OSBS are
CC biological functions (PubMed:24872444). {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_01933,
CC ECO:0000269|PubMed:24872444};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01933,
CC ECO:0000269|PubMed:24872444};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=59 uM for SHCHC {ECO:0000269|PubMed:24872444};
CC KM=640 uM for N-succinyl-L-phenylglycine
CC {ECO:0000269|PubMed:24872444};
CC Note=kcat is 170 sec(-1) with SHCHC as substrate. kcat is 1.6 sec(-1)
CC with N-succinyl-L-phenylglycine 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_01933}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01933}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24872444}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. MenC type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01933}.
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DR EMBL; AL596173; CAC97890.1; -; Genomic_DNA.
DR PIR; AB1765; AB1765.
DR RefSeq; WP_010991324.1; NC_003212.1.
DR PDB; 1WUF; X-ray; 2.90 A; A/B=1-374.
DR PDBsum; 1WUF; -.
DR SMR; Q927X3; -.
DR STRING; 272626.lin2664; -.
DR EnsemblBacteria; CAC97890; CAC97890; CAC97890.
DR KEGG; lin:lin2664; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_4_4_9; -.
DR OMA; DIVDHRH; -.
DR OrthoDB; 951991at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR EvolutionaryTrace; Q927X3; -.
DR Proteomes; UP000002513; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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:UniProtKB-UniRule.
DR CDD; cd03317; NAAAR; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_01933; MenC_2; 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; IPR013341; Mandelate_racemase_N_dom.
DR InterPro; IPR010197; OSB_synthase_MenC_2.
DR PANTHER; PTHR48073:SF5; PTHR48073:SF5; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01928; menC_lowGC/arch; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Lyase; Magnesium; Menaquinone biosynthesis;
KW Metal-binding.
FT CHAIN 1..374
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_0000455100"
FT ACT_SITE 164
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933"
FT STRAND 5..21
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 24..37
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1WUF"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:1WUF"
FT STRAND 361..368
FT /evidence="ECO:0007829|PDB:1WUF"
SQ SEQUENCE 374 AA; 42175 MW; 7670999F7CC12471 CRC64;
MYFQKARLIH AELPLLAPFK TSYGELKSKD FYIIELINEE GIHGYGELEA FPLPDYTEET
LSSAILIIKE QLLPLLAQRK IRKPEEIQEL FSWIQGNEMA KAAVELAVWD AFAKMEKRSL
AKMIGATKES IKVGVSIGLQ QNVETLLQLV NQYVDQGYER VKLKIAPNKD IQFVEAVRKS
FPKLSLMADA NSAYNREDFL LLKELDQYDL EMIEQPFGTK DFVDHAWLQK QLKTRICLDE
NIRSVKDVEQ AHSIGSCRAI NLKLARVGGM SSALKIAEYC ALNEILVWCG GMLEAGVGRA
HNIALAARNE FVFPGDISAS NRFFAEDIVT PAFELNQGRL KVPTNEGIGV TLDLKVLKKY
TKSTEEILLN KGWS
