ID   MENE_ENTFA              Reviewed;         485 AA.
AC   Q838K1;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=EF_0446;
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).
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}.
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DR   EMBL; AE016830; AAO80301.1; -; Genomic_DNA.
DR   RefSeq; NP_814230.1; NC_004668.1.
DR   RefSeq; WP_002387679.1; NZ_KE136524.1.
DR   AlphaFoldDB; Q838K1; -.
DR   SMR; Q838K1; -.
DR   STRING; 226185.EF_0446; -.
DR   EnsemblBacteria; AAO80301; AAO80301; EF_0446.
DR   KEGG; efa:EF0446; -.
DR   PATRIC; fig|226185.9.peg.411; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_0_9; -.
DR   OMA; WLMQRAF; -.
DR   BioCyc; MetaCyc:MON-13858; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00166.
DR   Proteomes; UP000001415; 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..485
FT                   /note="2-succinylbenzoate--CoA ligase"
FT                   /id="PRO_0000193160"
SQ   SEQUENCE   485 AA;  54289 MW;  1BAD82BCB5C08F82 CRC64;
     MTWLNKQVQK RPDHPAFYFQ DESWTFLEVQ QEVSHWVATY QQVLAPEEKR VALFSKNSKE
     LYFSILALWE LGKELLFLNT HLTLAELTFQ LKDAQVKTII GAPETQALLE EISFVDVQPM
     IKKQHSLSHQ EFQQPSDLES VASIMYTSGT TGQPKGVLQR FKNHLASARG TQENMGITAE
     DCWLCAVPLF HISGLSIVVR QLVLGCSIRL YDKFDEQQVT QDLQEGRGTV ISVVATMLQQ
     LLSVYPEAGY SASFKGMLLG GGPIAPDKLA QCEEKGIPVI QSYGMTETCS QVVALKFEDA
     ALKIGSAGQP LKDMQIKIVD ELGQEQPEKQ VGEILLKGPN VVSGYLNQRQ PEKWTADGWF
     KTGDMGYLDA QSYLYLVSRL SELIISGGEN IYPTEVEQVL QAITGIKAAA VVGEPDAQWG
     AVPVAYVISD QEITLAQIQD QCSRKLAKYK RPKRIYFCHS FPQTASGKIA KHRFMTEERE
     AFLIR