MENE_BACC7
ID MENE_BACC7 Reviewed; 481 AA.
AC B7HTW3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=BCAH187_A4993;
OS Bacillus cereus (strain AH187).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001177; ACJ78161.1; -; Genomic_DNA.
DR RefSeq; WP_000449584.1; NC_011658.1.
DR AlphaFoldDB; B7HTW3; -.
DR SMR; B7HTW3; -.
DR EnsemblBacteria; ACJ78161; ACJ78161; BCAH187_A4993.
DR KEGG; bcr:BCAH187_A4993; -.
DR HOGENOM; CLU_000022_59_0_9; -.
DR OMA; WLMQRAF; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR Proteomes; UP000002214; 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_1000132740"
SQ SEQUENCE 481 AA; 53545 MW; A37288E03699921A CRC64;
METMPNWLMQ RAFLTPDRTA IEIEEEKVTF MQLHEKVVSV CEHLTHVGVK RGQKVAVLMK
NGMEMITVIH ALSYVGAVAV LLNTRLSREE LLWQMDDAEV ICLVTDQDFD AKDIPVYSFA
EVMNGPKEEA SIQEEFSLEE AMTIIYTSGT TGKPKGVILT YGNHWASAVG SSLNLGLRDD
DCWLACMPMF HVGGLSLLMK NIMYGMRILL VPKYDADFIH KALQTRGVTI ISVVSKMLTD
LLERLGAETY PSSLRCMLLG GGPAPKPILE TCVEKGIPVY QTYGMTETSS QICTLSADYM
LTKVGSAGKP LFQCRLRIEK DGVVVPAFTE GEIVVKGPNV TGGYFNREDA TRETIQNGWL
HTGDLGYLDE EGFLYVLDRR SDLIISGGEN IYPAQIEEVL LSHPAVAEAG VVGMTDDKWG
QVPAAFVVKS GEVTEEEIIH FCEEKLAKYK VPKKACFLEE LPRNASKKLL RRELRQLVEE
M