ID MENE_BACP2 Reviewed; 486 AA.
AC A8FGK6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=BPUM_2715;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV63373.1; -; Genomic_DNA.
DR RefSeq; WP_012011000.1; NC_009848.4.
DR AlphaFoldDB; A8FGK6; -.
DR SMR; A8FGK6; -.
DR STRING; 315750.BPUM_2715; -.
DR KEGG; bpu:BPUM_2715; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_9; -.
DR OrthoDB; 9762242at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR Proteomes; UP000001355; 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 CDD; cd05912; OSB_CoA_lg; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR010192; MenE.
DR NCBIfam; TIGR01923; menE; 1.
DR PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Menaquinone biosynthesis; Nucleotide-binding.
FT CHAIN 1..486
FT /note="2-succinylbenzoate--CoA ligase"
FT /id="PRO_1000148089"
SQ SEQUENCE 486 AA; 54503 MW; 6294332D87B142ED CRC64;
MMKQPNWLLH RAYVTPERVA LIYQDKKWTF RDLADEVNEL SNRLAQTSLK KGEAVGLLMN
NHPQMVMLVH ACFSLGFKIV LLNNKLTKAE RRFQLEDVKA AALFTEPVYA SDHKGELPVY
TMETLPEAGQ ENVKKIENDF DLNQTATIMY TSGTTGRPKG VEQTFGNHFH SAVSSALNMG
LREDDRWLIA LPLFHISGLS ALFKSVIYGM TVVLHQKFDV DEVIGSIEQH RVTMISVVQT
MLSRLLSRLE ECPSSLRCLL LGGGPAPLAM LQESKEKGFP VFQSYGMTET CSQIVTLAPE
FSVEKLGSAG KPLFGCELKI QDGTRICRPF EHGEIMVKGA NVMKGYLYRE ESTAAAFDQG
WLKTGDIGYV DEEGFLFVLD RRSDLIISGG ENIYPAEIEA VLLTHSHVKE AGVTGIDDDR
WGEVPAAFLV TDHKIPENEL YALCESHLAK YKWPASFHFV DELPRNASNK LQRHRLKSKG
FLDDSN
//
