ID   MENE_BACC0              Reviewed;         482 AA.
AC   B7JDD6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 70.
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};
GN   OrderedLocusNames=BCAH820_4965;
OS   Bacillus cereus (strain AH820).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405535;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH820;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH820.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001283; ACK88096.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7JDD6; -.
DR   SMR; B7JDD6; -.
DR   EnsemblBacteria; ACK88096; ACK88096; BCAH820_4965.
DR   KEGG; bcu:BCAH820_4965; -.
DR   HOGENOM; CLU_000022_59_0_9; -.
DR   OMA; WLMQRAF; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00166.
DR   Proteomes; UP000001363; 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..482
FT                   /note="2-succinylbenzoate--CoA ligase"
FT                   /id="PRO_1000132739"
SQ   SEQUENCE   482 AA;  53682 MW;  59E0151CDF34C71C CRC64;
     MMETMPNWLK QRAFLTPDRT AIEIEEEKVT FMQLHEKVVS VCEHLTHVGV KRGQKVAVLM
     KNGIEMITVI HALSYAGAVA VLLNTRLSRE ELLWQMDDAE VICLVTDQDF EAKDIPVYSF
     AEVMNGPKEE ASIQEEFSLR EAMTIIYTSG TTGKPKGVIL TYGNHWASAV GSSLNLGLRD
     DDCWLACMPM FHVGGLSLLM KNIMYGMRIL LVPKYDADFI HKALQTRGVT IISVVSKMLT
     DLLERLGEGT YPSSLRCMLL GGGPAPKPLL ETCVDKGIPV YQTYGMTETS SQICTLSADY
     MLTKVGSAGK PLFQCQLRIE KDGVVVPPFA EGEIVVKGPN VTGGYFNRED ATRETIQNGW
     LHTGDLGYLD EEGFLYVLDR RSDLIISGGE NIYPAQIEEV LLSHPMVAEA GVVGMTDDKW
     GQVPAAFVVK SGEITEEEIL HFCEEKLAKY KVPKKACFLE ELPRNASKKL LRRELRQLVE
     EM