MENE_BACC1
ID MENE_BACC1 Reviewed; 481 AA.
AC Q72YK9;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=BCE_5012;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS43913.1; -; Genomic_DNA.
DR RefSeq; WP_000449580.1; NC_003909.8.
DR AlphaFoldDB; Q72YK9; -.
DR SMR; Q72YK9; -.
DR EnsemblBacteria; AAS43913; AAS43913; BCE_5012.
DR GeneID; 59158846; -.
DR KEGG; bca:BCE_5012; -.
DR HOGENOM; CLU_000022_59_0_9; -.
DR OMA; WLMQRAF; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR Proteomes; UP000002527; 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_0000193155"
SQ SEQUENCE 481 AA; 53501 MW; 3793025E6E60B078 CRC64;
METMPNWLMQ RAFLTPDRTA IEIEEEKVTF MQLHEKVVSV CEHLTHIGVK RGQKVAVLMK
NGMEMITVIH ALSYVGAVAV LLNTRLSREE LLWQMDDAEV ICLVTDQDFD AKDIPVYSFA
EVMNGPKEEA SIQEEFSLEE AMTIIYTSGT TGKPKGVILT YGNHWASAVG SSLNLGLRDD
DCWLACMPMF HVGGLSLLMK NIMYGMRILL VPKYDADFIH KALQTRGVTI ISVVSKMLTD
LLERLGAETY PSSLRCMLLG GGPAPKPLLE TCVEKGIPVY QTYGMTETSS QICTLSADYM
LTKVGSAGKP LFQCQLRIEK DGVVVPAFTE GEIVVKGPNV TGGYFNREDA TRETIQNGWL
HTGDIGYLDE EGFLYVLDRR SDLIISGGEN IYPAQIEEVL LSHPAVAEAG VVGMTDDKWG
QVPVAFVVKS GEVTEEEIIH FCEAKLAKYK VPKKACFLEE LPRNASKKLL RRELRQLVEE
M