ID C3T2M8_ECOLX Unreviewed; 451 AA.
AC C3T2M8;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
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=ECs3148 {ECO:0000313|EMBL:ACI80962.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI80962.1};
RN [1] {ECO:0000313|EMBL:ACI80962.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-24 {ECO:0000313|EMBL:ACI80962.1}, 87-14
RC {ECO:0000313|EMBL:ACI80963.1}, and TW14359
RC {ECO:0000313|EMBL:ACI80965.1};
RX PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA Sawyer S.A., Whittam T.S., Tarr P.I.;
RT "A precise reconstruction of the emergence and constrained radiations of
RT Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
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; EU898411; ACI80962.1; -; Genomic_DNA.
DR EMBL; EU898412; ACI80963.1; -; Genomic_DNA.
DR EMBL; EU898414; ACI80965.1; -; Genomic_DNA.
DR RefSeq; WP_000577566.1; NZ_VODI01000255.1.
DR AlphaFoldDB; C3T2M8; -.
DR PATRIC; fig|562.7073.peg.4344; -.
DR OMA; DCWLLSL; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
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; cd17630; OSB_MenE-like; 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|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00731};
KW Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428, ECO:0000256|HAMAP-
KW Rule:MF_00731}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00731}.
FT DOMAIN 11..317
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 366..423
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 451 AA; 50289 MW; 66707AB7128C65D2 CRC64;
MIFSDWPWRH WRQVRGEAIA LRLNDEQLNW RELCARVDEL ASGFAVQGVV EDSGVMLRAW
NTPQTLLAWL ALLQCGARVL PVNPQLPQPL LEELLPNLTL QFALVPDGEN TFPALTSLHI
QRVEGAHVAT WQPTRLCSMT LTSGSTGLPK AAVHTYQAHL ASAEGVLSLI PFGDHDDWLL
SLPLFHVSGQ GIMWRWLYAG ARMTVRDKQP LEQMLAGCTH ASLVPTQLWR LLVNRSSVSL
KAVLLGGAAI PVELTEQARE QGIRCFCGYG LTEFASTVCA KEADGLADVG SPLPGREVKI
VNNEVWLRAA SMAEGYWRNG QLVSLVNDEG WYATRDRGEM HNGKLTIVGR LDNLFFSGGE
GIQTEEVERV IAAHPAVLQV FIVPVADKEF GHRPVAVMEY DHESVDLSEW VKDKLARFQQ
PVRWLTLPPE LKNGGIKISR QALKEWVQRQ Q
//
