ID   MENE_SALTY              Reviewed;         455 AA.
AC   P37418;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 2.
DT   03-AUG-2022, entry version 127.
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=STM2305;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-455.
RC   STRAIN=LT2;
RX   PubMed=8206837; DOI=10.1128/jb.176.12.3589-3597.1994;
RA   Roland K.L., Esther C.R., Spitznagel J.K.;
RT   "Isolation and characterization of a gene, pmrD, from Salmonella
RT   typhimurium that confers resistance to polymyxin when expressed in multiple
RT   copies.";
RL   J. Bacteriol. 176:3589-3597(1994).
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; AE006468; AAL21206.1; -; Genomic_DNA.
DR   EMBL; U02281; AAA21323.1; -; Genomic_DNA.
DR   RefSeq; NP_461247.1; NC_003197.2.
DR   RefSeq; WP_000144677.1; NC_003197.2.
DR   AlphaFoldDB; P37418; -.
DR   SMR; P37418; -.
DR   STRING; 99287.STM2305; -.
DR   PaxDb; P37418; -.
DR   EnsemblBacteria; AAL21206; AAL21206; STM2305.
DR   GeneID; 1253827; -.
DR   KEGG; stm:STM2305; -.
DR   PATRIC; fig|99287.12.peg.2440; -.
DR   HOGENOM; CLU_000022_59_0_6; -.
DR   OMA; YHVSGLM; -.
DR   PhylomeDB; P37418; -.
DR   BioCyc; SENT99287:STM2305-MON; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00166.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR   GO; GO:0008756; F:o-succinylbenzoate-CoA ligase activity; IBA:GO_Central.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IBA:GO_Central.
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..455
FT                   /note="2-succinylbenzoate--CoA ligase"
FT                   /id="PRO_0000193176"
SQ   SEQUENCE   455 AA;  50244 MW;  BC830AB7BFAB0F42 CRC64;
     MTFTDWPWRH WRQVRSQAPA LRLNDEVLSW RALCERIDVL AGGFAAQGVR EGDGVLLRAG
     NQPRTLLAWL ALMQCGARVL PVNPQLPQTL LEALVPKLTL RFALTLEGEN AFSGLTALQI
     QKSTAAYAVA WQPQRLVSMT LTSGSTGLPK AAVHTCQAHL ASAQGVLSLM PFGPQDDWLL
     SLPLFHVSGQ GIMWRWLFAG ARMTVRDKQP LEQMLAGCTH ASLVPTQLWR LLANRAAVTL
     KAVLLGGAVI PVELTDQASK QGIRCWCGYG LTEFASTVCA KEADGSDDVG APLPGREIRI
     VDNEVWLRAA SMAEGYWRDG KLIPLVNDEG WFATRDRGEL NHGRLTIAGR LDNLFFSGGE
     GIQPEEVERV INAHPLVQQA FVVPVEDKEF GHRPVAVVEY ASQAGDVNLA EWVRDKLARF
     QQPVRWLTMP SELKNGGIKI SRRALQQWVC ENCKN