ID   MENE_MYCTO              Reviewed;         383 AA.
AC   P9WQ38; L0T3Z0; O06408; Q7D9P1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 3.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Probable 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=MT0567;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA
CC       (OSB-CoA). May be involved in the biosynthesis of menaquinone (By
CC       similarity). {ECO:0000250}.
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   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 5/7.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       MenE subfamily. {ECO:0000305}.
CC   -!- CAUTION: The predicted start codon is CTG.
CC       {ECO:0000250|UniProtKB:P9WQ39}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK44789.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000250|UniProtKB:P9WQ39};
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DR   EMBL; AE000516; AAK44789.1; ALT_INIT; Genomic_DNA.
DR   PIR; A70547; A70547.
DR   AlphaFoldDB; P9WQ38; -.
DR   SMR; P9WQ38; -.
DR   EnsemblBacteria; AAK44789; AAK44789; MT0567.
DR   KEGG; mtc:MT0567; -.
DR   HOGENOM; CLU_000022_59_3_11; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00166.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008756; F:o-succinylbenzoate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 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   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Menaquinone biosynthesis; Nucleotide-binding.
FT   CHAIN           1..383
FT                   /note="Probable 2-succinylbenzoate--CoA ligase"
FT                   /id="PRO_0000426843"
SQ   SEQUENCE   383 AA;  38755 MW;  DE5A26311FBACB61 CRC64;
     MRALHVPAGS ATALLLPALQ RVLGGSDPAL VAVPTQHESL LGALRVGEQI DDDVALVVTT
     SGTTGPPKGA MLTAAALTAS ASAAHDRLGG PGSWLLAVPP YHIAGLAVLV RSVIAGSVPV
     ELNVSAGFDV TELPNAIKRL GSGRRYTSLV AAQLAKALTD PAATAALAEL DAVLIGGGPA
     PRPILDAAAA AGITVVRTYG MSETSGGCVY DGVPLDGVRL RVLAGGRIAI GGATLAKGYR
     NPVSPDPFAE PGWFHTDDLG ALESGDSGVL TVLGRADEAI STGGFTVLPQ PVEAALGTHP
     AVRDCAVFGL ADDRLGQRVV AAIVVGDGCP PPTLEALRAH VARTLDVTAA PRELHVVNVL
     PRRGIGKVDR AALVRRFAGE ADQ