MENE_BACMK
ID MENE_BACMK Reviewed; 481 AA.
AC A9VM74;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 80.
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};
GN OrderedLocusNames=BcerKBAB4_4694;
OS Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBAB4;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY45847.1; -; Genomic_DNA.
DR RefSeq; WP_012261898.1; NC_010184.1.
DR AlphaFoldDB; A9VM74; -.
DR SMR; A9VM74; -.
DR STRING; 315730.BcerKBAB4_4694; -.
DR EnsemblBacteria; ABY45847; ABY45847; BcerKBAB4_4694.
DR KEGG; bwe:BcerKBAB4_4694; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_9; -.
DR OMA; WLMQRAF; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR Proteomes; UP000002154; 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.
FT CHAIN 1..481
FT /note="2-succinylbenzoate--CoA ligase"
FT /id="PRO_1000132741"
SQ SEQUENCE 481 AA; 53458 MW; 26B8A80AC068B9C4 CRC64;
METMPNWLMQ RAFLTPDRTA IEIEEEKVTF VQLHEKVVSV CEHLTHVGVK RAQKVAVLMK
NGMEMITVIH ALSYIGAVAV LLNTRLSREE LLWQMDDAEV VCLVTDQEFE TENVPVCSFA
EVMQGPKAEA FIQEEFSLEE AMTIIYTSGT TGKPKGVILT YGNHWASAVG SSLNLGLRDD
DCWLACMPMF HVGGLSLLMK NIMYGMRILL VPKYDANFIH KALQTRGVTI ISVVSKMLTD
LLERLGEGTY PSSLRCMLLG GGPAPKPLLE TCVEKGIPVY QTYGMTETSS QICTLTADYM
LTKVGSAGKP LFQCQLRIEK DGVVVPPRAE GEIVVKGPNV TGGYFNREDA THEAIRNGWL
HTGDLGYLDE EGFLYVLDRR SDLIISGGEN IYPAQIEEVL LSHPAVVEAG VVGMADESWG
QVPAAFVVKS GDVTEEEIIR FCEEKLAKYK VPKKACFLEE LPRNASKKLL RRELRKLVEE
M