MENC_STAAC
ID MENC_STAAC Reviewed; 333 AA.
AC A0A0H2WWB5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 44.
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=o-succinylbenzoic acid synthase {ECO:0000255|HAMAP-Rule:MF_01933};
GN Name=menC {ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000303|PubMed:24872444};
GN OrderedLocusNames=SACOL1843 {ECO:0000312|EMBL:AAW36861.1};
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2] {ECO:0007744|PDB:2OKT, ECO:0007744|PDB:2OLA, ECO:0007744|PDB:3H70}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 2-333 OF APOENZYME AND IN COMPLEX
RP WITH MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=COL;
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_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=287 uM for SHCHC {ECO:0000269|PubMed:24872444};
CC Note=kcat is 306 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_01933}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01933}.
CC -!- SUBUNIT: Monomer. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000046; AAW36861.1; -; Genomic_DNA.
DR RefSeq; WP_000778523.1; NC_002951.2.
DR PDB; 2OKT; X-ray; 1.30 A; A=2-333.
DR PDB; 2OLA; X-ray; 2.45 A; A=2-333.
DR PDB; 3H70; X-ray; 1.60 A; A=2-333.
DR PDBsum; 2OKT; -.
DR PDBsum; 2OLA; -.
DR PDBsum; 3H70; -.
DR SMR; A0A0H2WWB5; -.
DR EnsemblBacteria; AAW36861; AAW36861; SACOL1843.
DR KEGG; sac:SACOL1843; -.
DR HOGENOM; CLU_844431_0_0_9; -.
DR OMA; CRIINIK; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000000530; 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:UniProtKB-UniRule.
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; IPR010197; OSB_synthase_MenC_2.
DR PANTHER; PTHR48073:SF5; PTHR48073:SF5; 1.
DR Pfam; PF13378; MR_MLE_C; 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; Lyase; Magnesium; Menaquinone biosynthesis; Metal-binding.
FT CHAIN 1..333
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_0000455101"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933"
FT ACT_SITE 243
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933,
FT ECO:0000269|PubMed:24872444, ECO:0007744|PDB:3H70"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933,
FT ECO:0000269|PubMed:24872444, ECO:0007744|PDB:3H70"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933,
FT ECO:0000269|PubMed:24872444, ECO:0007744|PDB:3H70"
FT STRAND 3..20
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 25..38
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 61..75
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:2OKT"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:2OKT"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:2OKT"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2OKT"
SQ SEQUENCE 333 AA; 37968 MW; 9F68A03220CC1BF2 CRC64;
MKLTALHFYK YSEPFKSQIV TPKVTLTHRD CLFIELIDDK GNAYFGECNA FQTDWYDHET
IASVKHVIEQ WFEDNRNKSF ETYEAALKLV DSLENTPAAR ATIVMALYQM FHVLPSFSVA
YGATASGLSN KQLESLKATK PTRIKLKWTP QIMHQIRVLR ELDFHFQLVI DANESLDRQD
FTQLQLLARE QVLYIEEPFK DISMLDEVAD GTIPPIALDE KATSLLDIIN LIELYNVKVV
VLKPFRLGGI DKVQTAIDTL KSHGAKVVIG GMYEYGLSRY FTAMLARKGD YPGDVTPAGY
YFEQDVVAHS GILKEGRLEF RPPLVDITQL QPY
