ID A0A0N1CQW4_9ENTE Unreviewed; 483 AA.
AC A0A0N1CQW4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=2-succinylbenzoate--CoA ligase {ECO:0000256|HAMAP-Rule:MF_00731};
DE EC=6.2.1.26 {ECO:0000256|HAMAP-Rule:MF_00731};
DE AltName: Full=o-succinylbenzoyl-CoA synthetase {ECO:0000256|HAMAP-Rule:MF_00731};
DE Short=OSB-CoA synthetase {ECO:0000256|HAMAP-Rule:MF_00731};
GN Name=menE {ECO:0000256|HAMAP-Rule:MF_00731};
GN ORFNames=AEQ18_06290 {ECO:0000313|EMBL:KPG71229.1};
OS Enterococcus sp. RIT-PI-f.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1690244 {ECO:0000313|EMBL:KPG71229.1, ECO:0000313|Proteomes:UP000037898};
RN [1] {ECO:0000313|EMBL:KPG71229.1, ECO:0000313|Proteomes:UP000037898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT-PI-f {ECO:0000313|EMBL:KPG71229.1,
RC ECO:0000313|Proteomes:UP000037898};
RA Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT "Whole genome sequencing of endophytes isolated from poison ivy
RT (Toxicodendron radicans).";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA
CC (OSB-CoA). {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00731}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00731}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC MenE subfamily. {ECO:0000256|HAMAP-Rule:MF_00731}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPG71229.1}.
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DR EMBL; LHOX01000012; KPG71229.1; -; Genomic_DNA.
DR RefSeq; WP_054115517.1; NZ_LHOX01000012.1.
DR AlphaFoldDB; A0A0N1CQW4; -.
DR STRING; 1690244.AEQ18_06290; -.
DR PATRIC; fig|1690244.3.peg.2336; -.
DR OrthoDB; 9762242at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR Proteomes; UP000037898; Unassembled WGS sequence.
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; 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 {ECO:0000256|HAMAP-Rule:MF_00731};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00731, ECO:0000313|EMBL:KPG71229.1};
KW Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428, ECO:0000256|HAMAP-
KW Rule:MF_00731}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00731}.
FT DOMAIN 6..345
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 394..467
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 483 AA; 53615 MW; 186A50725CF58B13 CRC64;
MAGSWLQRQA QLHPERPAFY WQNKGWSFAA LQAEVQQYAA YYEAHLIAAQ RVAIYSENKP
EMVFTILALW ALGIEVQCLN TRLTNKELAF QLQDADCQLV ITDSRLDLAD VQLLPFGKKN
AVAFDIEDRL VYQSNQIASI MYTSGTTGKP KGVPQTFGNH QASAKATQQN LRISEEDCWL
CAVPLYHISG LSIVLRMVQL GISMRLYDRF DPKAMAADLA NSKGTVVSLV SKMLRDMLPY
VPQEGFLGLR YILLGGGPID RSLLEQCQHK QLSVIQSYGM TETCSQVVAL PPAKATAKLG
ASGIPLKGVQ LQIEDAKRHP ATAINEANRV GEIYLKGAAI VSSYLNARGC EQWNQEGWFA
TGDLGYLDEE GYLYVVSRSS ELIISGGENI YPAEVEQALQ QHPAVAEAAV VGQDNIQWGQ
EAVAFVVLKQ AVSKQALLDS LENRLAHYKF PRHIYQIDAL PRTASGKIIK RRLLSEERVN
EIE
//
