MENC_ENTFA
ID MENC_ENTFA Reviewed; 367 AA.
AC Q838J7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=EF_0450 {ECO:0000312|EMBL:AAO80305.1};
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2] {ECO:0007744|PDB:1WUE}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 700802 / V583;
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). Since the
CC gene is encoded in a menaquinone synthesis operon, OSB synthase is
CC probably the physiological activity. A pathway that requires NSAR
CC activity has not been identified in this species, so whether NSAR is
CC also a biological activity is unknown (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_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=72 uM for SHCHC {ECO:0000269|PubMed:24872444};
CC KM=170 uM for N-succinyl-L-phenylglycine
CC {ECO:0000269|PubMed:24872444};
CC Note=kcat is 120 sec(-1) with SHCHC as substrate. kcat is 24 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; AE016830; AAO80305.1; -; Genomic_DNA.
DR RefSeq; NP_814234.1; NC_004668.1.
DR RefSeq; WP_002387683.1; NZ_KE136524.1.
DR PDB; 1WUE; X-ray; 2.10 A; A/B=1-367.
DR PDBsum; 1WUE; -.
DR SMR; Q838J7; -.
DR STRING; 226185.EF_0450; -.
DR EnsemblBacteria; AAO80305; AAO80305; EF_0450.
DR KEGG; efa:EF0450; -.
DR PATRIC; fig|226185.45.peg.2885; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_4_4_9; -.
DR OMA; DIVDHRH; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR EvolutionaryTrace; Q838J7; -.
DR Proteomes; UP000001415; 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; Reference proteome.
FT CHAIN 1..367
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_0000455096"
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 3..21
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 24..38
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1WUE"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:1WUE"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:1WUE"
SQ SEQUENCE 367 AA; 41680 MW; CA624F6DCCC95878 CRC64;
MNIQSIETYQ VRLPLKTPFV TSYGRLEEKA FDLFVITDEQ GNQGFGELVA FEQPDYVQET
LVTERFIIQQ HLIPLLLTEA IEQPQEVSTI FEEVKGHWMG KAALETAIWD LYAKRQQKSL
TEFFGPTRRK IPVGISLGIQ EDLPQLLKQV QLAVEKGYQR VKLKIRPGYD VEPVALIRQH
FPNLPLMVDA NSAYTLADLP QLQRLDHYQL AMIEQPFAAD DFLDHAQLQR ELKTRICLDE
NIRSLKDCQV ALALGSCRSI NLKIPRVGGI HEALKIAAFC QENDLLVWLG GMFESGVGRA
LNLQFASQPT FSFPGDISAT ERYFYEDIIT EPFILEQGTM TVPQGLGIGV TLSQTNLLKY
SQYQKIM
