MENE_GEOSW
ID MENE_GEOSW Reviewed; 492 AA.
AC C5D6U5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=GWCH70_2796;
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC unclassified Geobacillus.
OX NCBI_TaxID=471223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) 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}.
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DR EMBL; CP001638; ACS25484.1; -; Genomic_DNA.
DR RefSeq; WP_015864888.1; NC_012793.1.
DR AlphaFoldDB; C5D6U5; -.
DR SMR; C5D6U5; -.
DR STRING; 471223.GWCH70_2796; -.
DR PRIDE; C5D6U5; -.
DR EnsemblBacteria; ACS25484; ACS25484; GWCH70_2796.
DR KEGG; gwc:GWCH70_2796; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_9; -.
DR OMA; WLMQRAF; -.
DR OrthoDB; 377638at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
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..492
FT /note="2-succinylbenzoate--CoA ligase"
FT /id="PRO_1000212735"
SQ SEQUENCE 492 AA; 54899 MW; 9428938AA3783635 CRC64;
MQTSIPNWLM QRAFLTPERI AVYDGQGKKT FMELHESVMK RARQLANTGV RKGDIVAIFM
KNSVAMIECI HALHYIGAIV LLQNTRLTSH ELAWQLKDSG AVYVIADDEL ADRIEGNIRV
ITMSELSALP EENVEFQQYY HFDDIATIMY TSGTTGKPKG VLQTYENHWW SAIGSALNLG
LNENDCWLAA VPFFHISGLS IMMRSVIYGM SMYVMRAFDA KKANELIIGG KVTIMSVVSA
MLQKMIADLG ERRYPETFRC MLLGGGPAPK PLLEVCKAKG IPVYQTYGMT ETASQIATLA
PEYSLTKLGS AGKPLFPSQL RIEKDGQVAR PYEPGEIVVK GPNVTKGYLH RPDATAKAIR
GGWFYTGDIG YIDEDGFLYV LDRRSDLIIS GGENVYPAEI EAVLLSHEAV EEAGVTGIDD
ETWGQVPCAF VKRKRGYSVT VEQLKQFCQA HLAKYKIPKQ IYFVDELPRN ASQKLLRHQL
KQLIPNNENG AL