ID   MENE_BACAC              Reviewed;         482 AA.
AC   C3LB87;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=BAMEG_5142;
OS   Bacillus anthracis (strain CDC 684 / NRRL 3495).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=568206;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 684 / NRRL 3495;
RA   Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C.,
RA   Sutton G., Sims D.;
RT   "Genome sequence of Bacillus anthracis str. CDC 684.";
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; CP001215; ACP12427.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3LB87; -.
DR   SMR; C3LB87; -.
DR   KEGG; bah:BAMEG_5142; -.
DR   HOGENOM; CLU_000022_59_0_9; -.
DR   OMA; WLMQRAF; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00166.
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_1000148087"
SQ   SEQUENCE   482 AA;  53748 MW;  145D7170323C1FAB CRC64;
     MMETMPNWLK QRAFLTPDRT AIEIEEEKVT FMQLHEKVVS VCEHLTHVGV NRGQKVAVLM
     KNGMEMITVI HALSYVGAVA VLLNTRLSRE ELLWQMDDAE VICLVTDQDF EAKDIPVYSF
     AEVMNGPKEE ASIQEEFSLR EAMTIIYTSG TTGKPKGVIL TYGNHWASAV GSSLNLGLRD
     DDCWLACMPM FHVGGLSLLM KNIMYGMRIL LVPKYDADFI HKALQTRGVT IISVVSKMLT
     DLLERLGEGT YPSSFRCMLL GGGPAPKPLL ETCVDKGIPV YQTYGMTETS SQICTLSADY
     MLTKVGSAGK PLFQCQLRIE KDGVVVPPFA EGEIVVKGPN VTGGYFNRED ATRETIQNGW
     LHTGDLGYLD EEGFLYVLDR RSDLIISGGE NIYPAQIEEV LLSHPMVAEA GVVGMTDDKW
     GQVPAAFVVK SGEITEEEIL HFCEEKLAKY KVPKKACFLE ELPRNASKKL LRRELRQLVE
     EM