MENE_LACLA
ID MENE_LACLA Reviewed; 451 AA.
AC Q9CHK3;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 2.
DT 25-MAY-2022, entry version 109.
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=LL0728;
GN ORFNames=L0172;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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=AAK04826.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005176; AAK04826.1; ALT_INIT; Genomic_DNA.
DR PIR; H86715; H86715.
DR RefSeq; NP_266884.2; NC_002662.1.
DR RefSeq; WP_010905533.1; NC_002662.1.
DR AlphaFoldDB; Q9CHK3; -.
DR SMR; Q9CHK3; -.
DR STRING; 272623.L0172; -.
DR PaxDb; Q9CHK3; -.
DR DNASU; 1114354; -.
DR EnsemblBacteria; AAK04826; AAK04826; L0172.
DR KEGG; lla:L0172; -.
DR PATRIC; fig|272623.7.peg.781; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_9; -.
DR OMA; WLMQRAF; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR Proteomes; UP000002196; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Menaquinone biosynthesis; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..451
FT /note="2-succinylbenzoate--CoA ligase"
FT /id="PRO_0000193161"
SQ SEQUENCE 451 AA; 50578 MW; D0F4EE4619182346 CRC64;
MKWLKKQAEL YPQKQFLNDS TFAQINQEVN KMAEHLAPLI DNQSRVALLS ENSVEMAVVL
FALLGLSKEV LLLNRHLTEY ELADQIKELK IDKVFTSDLL TEKVTDSISF SEIWTSNPCP
VSLSADFPDE KIAVIMNTSA TTGKFKSVPI TWGMISNHVK ASKETLGAYD NDNWLVILPM
FHVSGLSIIM RTLYNATSAT VVDKFDENQL LEMINSGKIN MVSLVPTLLT RIADKLHSNN
LRLILLGGEF IPQPLIKKCQ ELGLPIYKTY GMTESFSQSV TFNILDFPDK TSSVGRPLPG
VEIEIRQADL AGVGEIWLKS PMLMKAYLGQ KPYGTAFETG DIGYLDTDGF LYLLNRRKDI
IISGGENIYP KEIEDLVYSL PEIKECALVA KPDAKWGQVP ILFVSGNISQ EKLENFLTEK
LAKYKRPQSI TFMDELPKNA SGKILRKELK G