ID   MENE_OCEIH              Reviewed;         480 AA.
AC   Q8ENZ7;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=OB2322;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC14278.1; -; Genomic_DNA.
DR   RefSeq; WP_011066715.1; NC_004193.1.
DR   AlphaFoldDB; Q8ENZ7; -.
DR   SMR; Q8ENZ7; -.
DR   STRING; 221109.22778007; -.
DR   EnsemblBacteria; BAC14278; BAC14278; BAC14278.
DR   KEGG; oih:OB2322; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_0_9; -.
DR   OMA; WLMQRAF; -.
DR   OrthoDB; 377638at2; -.
DR   PhylomeDB; Q8ENZ7; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00166.
DR   Proteomes; UP000000822; 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..480
FT                   /note="2-succinylbenzoate--CoA ligase"
FT                   /id="PRO_0000193165"
SQ   SEQUENCE   480 AA;  54018 MW;  CB2BE59F532FCB9F CRC64;
     MSETTPHWLT KRADLSPDKK AIEFEDGSSI TYLELFHRSQ SYARKLGKLG FRQGDHIAIL
     STNCAEMIQI IYACSYLGAV AVLLNTKLTI NELNQQLLDS DAKVIITSES FKASEFVLQR
     MDYNELESVT EDTSIITLKS EIYFDDIFTM MYTSGTTGFP KAVQQTFGNH WWSATSSALN
     LGLHDNDKWL IPLPLFHVSG LSTMLKSVIY GMPIYVLEKF EVEKVHNAIM DRKVTIVSVV
     TVMVQRLIKR LGNHHYPNDF RCMLLGGGPA PKSLLEQAKL KNIPVFQSYG MTETSSQIVT
     LTPEDALKKI GSAGKPLFPA QLKIAHNENN PNQIGEILVK GPMVTKGYYK RAETNKEVFE
     NNWLHTGDMG YLDEQGYLYV VDRRNDLIIS GGENIYPSEI ENVLVQIEGI EEAGVKGSPN
     EEWGMVPIAF IVCSRPISEN EIAAHLEKYL AKYKRPKEIH VVNELPRNAA NKLVRHNLGK