ID   MENE_LISMO              Reviewed;         467 AA.
AC   P58730; Q8Y6L2;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=2-succinylbenzoate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_00731};
DE            EC=6.2.1.26 {ECO:0000255|HAMAP-Rule:MF_00731};
DE   AltName: Full=o-succinylbenzoyl-CoA synthetase {ECO:0000255|HAMAP-Rule:MF_00731};
DE            Short=OSB-CoA synthetase {ECO:0000255|HAMAP-Rule:MF_00731};
GN   Name=menE {ECO:0000255|HAMAP-Rule:MF_00731}; OrderedLocusNames=lmo1672;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
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).
CC   -!- FUNCTION: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA
CC       (OSB-CoA). {ECO:0000255|HAMAP-Rule:MF_00731}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-succinylbenzoate + ATP + CoA = 2-succinylbenzoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:17009, ChEBI:CHEBI:18325,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57364, ChEBI:CHEBI:456215; EC=6.2.1.26;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00731};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 5/7.
CC       {ECO:0000255|HAMAP-Rule:MF_00731}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00731}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       MenE subfamily. {ECO:0000255|HAMAP-Rule:MF_00731}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC99750.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL591980; CAC99750.1; ALT_INIT; Genomic_DNA.
DR   PIR; AH1283; AH1283.
DR   RefSeq; NP_465197.1; NC_003210.1.
DR   AlphaFoldDB; P58730; -.
DR   SMR; P58730; -.
DR   STRING; 169963.lmo1672; -.
DR   PaxDb; P58730; -.
DR   EnsemblBacteria; CAC99750; CAC99750; CAC99750.
DR   GeneID; 985655; -.
DR   KEGG; lmo:lmo1672; -.
DR   PATRIC; fig|169963.11.peg.1715; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_0_9; -.
DR   PhylomeDB; P58730; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00166.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008756; F:o-succinylbenzoate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   HAMAP; MF_00731; MenE; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR010192; MenE.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR01923; menE; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Menaquinone biosynthesis; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..467
FT                   /note="2-succinylbenzoate--CoA ligase"
FT                   /id="PRO_0000193164"
SQ   SEQUENCE   467 AA;  51874 MW;  0031E3A166F4CBDA CRC64;
     MTNWLQKRVR LSPKETALVF EGKEETFEEI SEAVERLAGK LFALGIRKDE MIALLGKNDR
     MTFLLIHALQ QLGAVTLFLN NRLTKKEIAY QLANAEVKQV IVADTFEDKV GAGISYSELA
     ETDYKEPELL ETWDLSRTAS IMYTSGTTGK PKGVIQTYEN HWWSAVASVL NLGLTEKDSW
     LCAVPIFHIS GLSIMMRSVI YGIPVYLEEH FDEEKITQLL ESGKVSTISV VTSMLERLLK
     IHGGSYHPNV RTILLGGGPA SKTVLEICKQ RDIPLVQSFG MTETASQIVT LPPKDALNKI
     GSSGKALFPA EVKIADDGEI LLKGPSITPG YLHNKKATEA SFVDGWFKTG DIGYLDEEGF
     LFVVERRSDL IISGGENIYP TEIEHVIGEY VAVKEVAVIG QPDDKWGSVP VAFIVAEETF
     DEDELQLICQ TNLASYKIPK QIIIVEKLPK TASGKIQRNK LKERHSK