MENE_GEOKA
ID MENE_GEOKA Reviewed; 490 AA.
AC Q5KVX9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=GK2872;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(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; BA000043; BAD77157.1; -; Genomic_DNA.
DR RefSeq; WP_011232344.1; NC_006510.1.
DR AlphaFoldDB; Q5KVX9; -.
DR SMR; Q5KVX9; -.
DR STRING; 235909.GK2872; -.
DR EnsemblBacteria; BAD77157; BAD77157; GK2872.
DR KEGG; gka:GK2872; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_7_9; -.
DR OMA; WLMQRAF; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR Proteomes; UP000001172; 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..490
FT /note="2-succinylbenzoate--CoA ligase"
FT /id="PRO_1000045964"
SQ SEQUENCE 490 AA; 54012 MW; D454FADF55B9C7A2 CRC64;
MTTMPNWLKQ RAFLTPERIA VSDGRRTKTF AELYEAAAVW ARRLAQAGVK EGDIVALLMK
NRIEMIEIIH ALFFLGARVL LQNVRLTSYE LGWQLDDSGA RLAIADEELA GSLDGDGRVL
TVGAVAALPE VDVSLKETCD LEEVATIMYT SGTTGTPKGV LQTYGNHWWS AVGSALNLGL
HERDCWLAAV PLFHISGLSI AMRSVIYGMP MRLQTSFDPK EANEWIMRGD VTIMSVVAAM
LQRMVAELGE ARYPDTFRCM LLGGGPAPRP LLEACKEKGI PVYQTYGMTE TASQIATLAP
EYSLTKLGSA GKPLFPAELC ILKDGKPAAP HEAGEIVVKG PNVTKGYWQR PEATAQAIRG
GWFFTGDIGY LDEDGFLYVL DRRSDLIISG GENVYPAEVE AVLLSHPDVE EAGVTGVENE
TWGQVPYAFV RLKRGASPDE AALRAFCRER LAKYKVPARI YFVDELPRNA AQKLLRRELK
RLIPKTEQTF