ID   MENE_BACP2              Reviewed;         486 AA.
AC   A8FGK6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=BPUM_2715;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV63373.1; -; Genomic_DNA.
DR   RefSeq; WP_012011000.1; NC_009848.4.
DR   AlphaFoldDB; A8FGK6; -.
DR   SMR; A8FGK6; -.
DR   STRING; 315750.BPUM_2715; -.
DR   EnsemblBacteria; ABV63373; ABV63373; BPUM_2715.
DR   KEGG; bpu:BPUM_2715; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_0_9; -.
DR   OMA; WLMQRAF; -.
DR   OrthoDB; 377638at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00166.
DR   Proteomes; UP000001355; 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..486
FT                   /note="2-succinylbenzoate--CoA ligase"
FT                   /id="PRO_1000148089"
SQ   SEQUENCE   486 AA;  54503 MW;  6294332D87B142ED CRC64;
     MMKQPNWLLH RAYVTPERVA LIYQDKKWTF RDLADEVNEL SNRLAQTSLK KGEAVGLLMN
     NHPQMVMLVH ACFSLGFKIV LLNNKLTKAE RRFQLEDVKA AALFTEPVYA SDHKGELPVY
     TMETLPEAGQ ENVKKIENDF DLNQTATIMY TSGTTGRPKG VEQTFGNHFH SAVSSALNMG
     LREDDRWLIA LPLFHISGLS ALFKSVIYGM TVVLHQKFDV DEVIGSIEQH RVTMISVVQT
     MLSRLLSRLE ECPSSLRCLL LGGGPAPLAM LQESKEKGFP VFQSYGMTET CSQIVTLAPE
     FSVEKLGSAG KPLFGCELKI QDGTRICRPF EHGEIMVKGA NVMKGYLYRE ESTAAAFDQG
     WLKTGDIGYV DEEGFLFVLD RRSDLIISGG ENIYPAEIEA VLLTHSHVKE AGVTGIDDDR
     WGEVPAAFLV TDHKIPENEL YALCESHLAK YKWPASFHFV DELPRNASNK LQRHRLKSKG
     FLDDSN