ID A0A1G9QNV5_9BACI Unreviewed; 495 AA.
AC A0A1G9QNV5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN05216244_1594 {ECO:0000313|EMBL:SDM12689.1};
OS Sediminibacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Sediminibacillus.
OX NCBI_TaxID=482461 {ECO:0000313|EMBL:SDM12689.1, ECO:0000313|Proteomes:UP000182347};
RN [1] {ECO:0000313|EMBL:SDM12689.1, ECO:0000313|Proteomes:UP000182347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6199 {ECO:0000313|EMBL:SDM12689.1,
RC ECO:0000313|Proteomes:UP000182347};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNHF01000002; SDM12689.1; -; Genomic_DNA.
DR RefSeq; WP_074598336.1; NZ_FNHF01000002.1.
DR AlphaFoldDB; A0A1G9QNV5; -.
DR STRING; 482461.SAMN05216244_1594; -.
DR OrthoDB; 9762242at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR Proteomes; UP000182347; 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 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 {ECO:0000256|HAMAP-Rule:MF_00731};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00731, ECO:0000313|EMBL:SDM12689.1};
KW Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428, ECO:0000256|HAMAP-
KW Rule:MF_00731};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00731}.
FT DOMAIN 10..356
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 406..480
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 495 AA; 54214 MW; BA94E0B42A0E7E14 CRC64;
MTEVIPHWLD KQADLSPDKT AIETSDGEEL TFQQLRDKSR SLAKKMAASG VQEGNHVALL
AANSSDMAAA IHALSYLGAV AVLLNVRLSA AELAYQLNDA EVSCLLYDDG HTELALSAVD
QADCPDFRSF REIIEQTETT VALQEELVLN KLFTIIYTSG TTGFPKGVEH TYGNHWWSAV
SSALNLGLSK NDKWLASLPL FHVGGLSLLV KSVVYGMPVY LMKKFDIDLA HRAIISENVT
IVSVVAVMLE RLINKLAGGR YPDSFRCMLL GGGPAPEPLL EKARLHEIPV FQTYGMTETS
SQIVTLSPDY ALSKLGSAGK PLVPAQLKIM LEGNPAPDGT VGEIVVKGPM VTKGYYKNDS
ANDKSFHDGW LATGDLGKLD EDGFLYVMDR RKDLIISGGE NIYPAEIESV LAGMDGVKEA
GVIGREDDQW GQVPVVFIVA SHTDLTKEKV FDYCRERLAK FKVPKHVYFI AELPRNASNK
LVRHKLVDLL GEYES
//
