ID A0A2X4T8E4_SALER Unreviewed; 455 AA.
AC A0A2X4T8E4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:SQI22689.1};
GN ORFNames=NCTC7307_01861 {ECO:0000313|EMBL:SQI22689.1};
OS Salmonella enterica subsp. arizonae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=59203 {ECO:0000313|EMBL:SQI22689.1, ECO:0000313|Proteomes:UP000248731};
RN [1] {ECO:0000313|EMBL:SQI22689.1, ECO:0000313|Proteomes:UP000248731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC7307 {ECO:0000313|EMBL:SQI22689.1,
RC ECO:0000313|Proteomes:UP000248731};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; LS483466; SQI22689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X4T8E4; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR Proteomes; UP000248731; Chromosome 1.
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:SF10; SURFACTIN SYNTHASE SUBUNIT 1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000248731}.
FT DOMAIN 11..317
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 366..424
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 455 AA; 50418 MW; AEFDE6732F4CEB04 CRC64;
MTFTDWPWRH WRQVRSQAPA LRLNDEVLSW RALCERIDVL AGGFAAQGVR ESDGVLLRAW
NHPHTLLAWL ALMQCGARVL PVNPQLPQSL LEALVPELTL RFALTLEGEN AFSGLTALQM
RKSTEAYAVA WQPQRLVSMT LTSGSTGLPK AAIHTYRAHL ASAQGVLSLM PFGPQDDWLL
SLPLFHVSGQ GIMWRWLFAG ARMTVRDKQP LEQMLAGCTH ASLVPTQLWR LLANQAAVTL
KAVLLGGAVI PVELTNQASR QGIRCWCGYG LTEFASTVCA KEADGSDDVG APLPGREVRI
VDNEVWLRAA SMAEGYWRDG KLIPLVNDEG WFATRDRGAL NHGRLTIAGR LDNLFFSGGE
GIQPEEVERI INAHPLVQQA FVVPVEDKEF GHRPVAVVEY VSQAGEVNLA EWVSDKLARF
QQPVRWLTLP PELKNGGIKI SRRALQQWVC KSGKN
//
