ID   MENE_LISIN              Reviewed;         467 AA.
AC   Q92AY8;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   25-MAY-2022, entry version 119.
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=lin1780;
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).
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=CAC97011.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL596169; CAC97011.1; ALT_INIT; Genomic_DNA.
DR   PIR; AC1655; AC1655.
DR   RefSeq; WP_010990951.1; NC_003212.1.
DR   AlphaFoldDB; Q92AY8; -.
DR   SMR; Q92AY8; -.
DR   STRING; 272626.lin1780; -.
DR   EnsemblBacteria; CAC97011; CAC97011; CAC97011.
DR   KEGG; lin:menE; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_0_9; -.
DR   OrthoDB; 377638at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00166.
DR   Proteomes; UP000002513; 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.
FT   CHAIN           1..467
FT                   /note="2-succinylbenzoate--CoA ligase"
FT                   /id="PRO_0000193162"
SQ   SEQUENCE   467 AA;  51712 MW;  3DB2D8A46617E745 CRC64;
     MTNWLQKRVR LSPGETALVF EGKQETFEEI YEAVEKLAGK LFARGIRKDE MVALLGKNDR
     MTFLLIHALQ QLGAITLFLN NRLTKKEITF QLANAEVKQV IVADAFVDKV TSGISYEELQ
     QTTYVEPDLC KTWDLSRTAS VMYTSGTTGK PKGVMQTYEN HWWSAVSSVL NLGLTEKDSW
     LCAVPIFHIS GLSIMMRSVI YGIPVYLEEH FDEEKITQLL ESGKISTISV VTSMLERLLK
     IQGGSYHPNV RTVLLGGGPA NKAVLEICKQ RDIPLVQSFG MTETASQIVT LPPKDALNKI
     GSSGKALFPA EVKIADDGEI LLKGPSITPG YLHNEKATAK AFIDGWFKTG DIGYLDEEGF
     LFVLERRSDL IISGGENIYP TEIEHVIGAY EAVEEVAVVG KSDAKWGSVP VAFIVVNEGF
     DEGVLKDICQ TNLASFKIPK QITIVEHLPK TASGKIQRNK LKERHSN