ID   C1EX40_BACC3            Unreviewed;       482 AA.
AC   C1EX40;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   01-MAY-2013, entry version 33.
DE   RecName: Full=2-succinylbenzoate--CoA ligase;
DE            EC=6.2.1.26;
DE   AltName: Full=OSB-CoA synthetase;
DE   AltName: Full=o-succinylbenzoyl-CoA synthetase;
GN   Name=menE; OrderedLocusNames=BCA_4988;
OS   Bacillus cereus (strain 03BB102).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=572264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03BB102;
RA   Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA   Tapia R., Han C., Sutton G., Sims D.;
RT   "Genome sequence of Bacillus cereus 03BB102.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-
CC       CoA (OSB-CoA) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + 2-succinylbenzoate + CoA = AMP +
CC       diphosphate + 2-succinylbenzoyl-CoA.
CC   -!- PATHWAY: Cofactor biosynthesis; menaquinone biosynthesis;
CC       menaquinone-2 from chorismate: step 5/8.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. MenE subfamily.
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DR   EMBL; CP001407; ACO27377.1; -; Genomic_DNA.
DR   RefSeq; YP_002752230.1; NC_012472.1.
DR   ProteinModelPortal; C1EX40; -.
DR   STRING; 572264.BCA_4988; -.
DR   EnsemblBacteria; ACO27377; ACO27377; BCA_4988.
DR   GeneID; 7691793; -.
DR   KEGG; bcx:BCA_4988; -.
DR   PATRIC; 18823135; VBIBacCer84800_4881.
DR   eggNOG; COG0318; -.
DR   HOGENOM; HOG000230005; -.
DR   KO; K01911; -.
DR   OMA; LRCMLLG; -.
DR   ProtClustDB; PRK03640; -.
DR   BioCyc; BCER572264:GH22-1738-MONOMER; -.
DR   UniPathway; UPA00079; UER00166.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008756; F:o-succinylbenzoate-CoA ligase activity; IEA:HAMAP.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00731; MenE; 1; -.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR025110; DUF4009.
DR   InterPro; IPR010192; MenE.
DR   InterPro; IPR023015; SB_CoA_ligase_firmicutes.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; DUF4009; 1.
DR   TIGRFAMs; TIGR01923; menE; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Menaquinone biosynthesis;
KW   Nucleotide-binding.
SQ   SEQUENCE   482 AA;  53811 MW;  2639ADA35EBBAF0D CRC64;
     MMETMPNWLK QRAFLTPDRT AIEIEEEKVT FMQLHEKVVS VCEHLTYVGV KRGQKVAVLM
     KNGMEMITVI HALSYVGAVA VLLNTRLSRE ELLWQMDDAE VVCLVTDQDF EAKDVLVYSF
     TEIMNGPKAK ASIQEDFSLE EAMTIIYTSG TTGKPKGVIL TYGNHWASAI GSSLNLGLRD
     NDCWLACMPM FHVGGLSLLM KNIMYGMRIL LVPKYDADFI HKALQTRGVT IISVVSKMLT
     DLLERLGEET YPSSLRCMLL GGGPAPKPLL ETCVEKGIPV YQTYGMTETS SQICTLSADY
     MLTKVGSAGK PLFQCQLRIE KDGVVVAPRT EGEIVVKGPN VTGGYFNRED ATRETIQNGW
     LHTGDLGYLD EEGFLYVLDR RSDLIISGGE NIYPAQIEEV LLSHPMVAEA GVVGMTDDKW
     GQVPAAFVVK NGEVTEEEIL HFCEEKLAKY KVPKKACFLE ELPRNASKKL LRRELRQLVE
     EM
//