MENE_BACAN
ID MENE_BACAN Reviewed; 481 AA.
AC Q81K97; Q6HRP7; Q6KL14;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 126.
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=BA_5108, GBAA_5108, BAS4747;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) 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 -!- SEQUENCE CAUTION:
CC Sequence=AAT57041.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016879; AAP28780.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34234.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT57041.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_847294.1; NC_003997.3.
DR RefSeq; WP_000449553.1; NZ_WXXJ01000032.1.
DR RefSeq; YP_030991.1; NC_005945.1.
DR AlphaFoldDB; Q81K97; -.
DR SMR; Q81K97; -.
DR IntAct; Q81K97; 4.
DR STRING; 260799.BAS4747; -.
DR DNASU; 1084412; -.
DR EnsemblBacteria; AAP28780; AAP28780; BA_5108.
DR EnsemblBacteria; AAT34234; AAT34234; GBAA_5108.
DR GeneID; 45024714; -.
DR KEGG; ban:BA_5108; -.
DR KEGG; bar:GBAA_5108; -.
DR KEGG; bat:BAS4747; -.
DR PATRIC; fig|198094.11.peg.5069; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_9; -.
DR OMA; WLMQRAF; -.
DR BRENDA; 6.2.1.26; 634.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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;
KW Reference proteome.
FT CHAIN 1..481
FT /note="2-succinylbenzoate--CoA ligase"
FT /id="PRO_0000193154"
SQ SEQUENCE 481 AA; 53617 MW; 9C536CD117D1BE8E CRC64;
METMPNWLKQ RAFLTPDRTA IEIEEEKVTF MQLHEKVVSV CEHLTHVGVN RGQKVAVLMK
NGMEMITVIH ALSYVGAVAV LLNTRLSREE LLWQMDDAEV ICLVTDQDFE AKDIPVYSFA
EVMNGPKEEA SIQEEFSLRE AMTIIYTSGT TGKPKGVILT YGNHWASAVG SSLNLGLRDD
DCWLACMPMF HVGGLSLLMK NIMYGMRILL VPKYDADFIH KALQTRGVTI ISVVSKMLTD
LLERLGEGTY PSSFRCMLLG GGPAPKPLLE TCVDKGIPVY QTYGMTETSS QICTLSADYM
LTKVGSAGKP LFQCQLRIEK DGVVVPPFAE GEIVVKGPNV TGGYFNREDA TRETIQNGWL
HTGDLGYLDE EGFLYVLDRR SDLIISGGEN IYPAQIEEVL LSHPMVAEAG VVGMTDDKWG
QVPAAFVVKS GEITEEEILH FCEEKLAKYK VPKKACFLEE LPRNASKKLL RRELRQLVEE
M
