ID A0A3Q9QZ08_9BACI Unreviewed; 496 AA.
AC A0A3Q9QZ08;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 ECO:0000313|EMBL:AZU63689.1};
GN ORFNames=CHR53_21780 {ECO:0000313|EMBL:AZU63689.1};
OS Neobacillus mesonae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1193713 {ECO:0000313|EMBL:AZU63689.1, ECO:0000313|Proteomes:UP000282892};
RN [1] {ECO:0000313|EMBL:AZU63689.1, ECO:0000313|Proteomes:UP000282892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H20-5 {ECO:0000313|EMBL:AZU63689.1,
RC ECO:0000313|Proteomes:UP000282892};
RA Kim S.Y., Song H., Sang M.K., Weon H.-Y., Song J.;
RT "The complete genome sequence of Bacillus mesonae strain H20-5, an
RT efficient strain improving plant abiotic stress resistance.";
RL Submitted (JUL-2017) 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; CP022572; AZU63689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q9QZ08; -.
DR STRING; 1193713.GCA_001636315_01239; -.
DR KEGG; nmk:CHR53_21780; -.
DR OrthoDB; 9762242at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR Proteomes; UP000282892; 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 {ECO:0000256|HAMAP-Rule:MF_00731};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00731, ECO:0000313|EMBL:AZU63689.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000282892}.
FT DOMAIN 12..355
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 405..480
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 496 AA; 55732 MW; DCC62ED6AEF84A79 CRC64;
MQTMPNFLMK RAFLTPERIA VYFRDQAITF EELYILSVTT AGQLQKLGVK KDQFIAVLLK
NHLDTVVILF ALQLLGVKTV ILNNRLTPAE LAWQLKDSKV SALILDDVFS HLEQMLSQEL
SSLHTFTKTN LFSQESISTE LQEEISLDEI CTIMYTSGTT GNPKGVMQTY GNHWWSATGS
ALNLGVTDQD CWLCTVPLFH ISGFSILMRS VIYGMPLVLH EKFDQERTIQ DIKEKKVTIM
SVVGTMLTRI VESLKGGQLP QQFRCMLLGG GPAPLPLLKA CVEKQIPVFQ TYGMTETSSQ
IVTLSPEYSL SKLGSAGKPL FPSEIRIERT EGSKAQPGEA GEIIVKGPNV TRGYLYRPDA
TEDKIRNGWL YTGDIGYLDE DGFLYVLDRR SDLIISGGEN IYPAEIEAVL LAHPEIQEAG
VTGLNDPRWG QVPVAFIVTK NGEELSSDEL KQFCREQLAK YKVPKDFYFT DQLPRNAAKK
LLRRTLKEWL DEGRFK
//
