MENE_ECOLI
ID MENE_ECOLI Reviewed; 451 AA.
AC P37353; P78178; P78253;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=2-succinylbenzoate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_00731};
DE EC=6.2.1.26 {ECO:0000255|HAMAP-Rule:MF_00731};
DE AltName: Full=o-succinylbenzoyl-CoA synthetase {ECO:0000255|HAMAP-Rule:MF_00731};
DE Short=OSB-CoA synthetase {ECO:0000255|HAMAP-Rule:MF_00731};
GN Name=menE {ECO:0000255|HAMAP-Rule:MF_00731};
GN OrderedLocusNames=b2260, JW2255;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION AS AN O-SUCCINYLBENZOYL-COA
RP SYNTHASE.
RC STRAIN=K12;
RX PubMed=8626063; DOI=10.1016/0378-1119(95)00721-0;
RA Sharma V., Hudspeth M.E.S., Meganathan R.;
RT "Menaquinone (vitamin K2) biosynthesis: localization and characterization
RT of the menE gene from Escherichia coli.";
RL Gene 168:43-48(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA
CC (OSB-CoA). {ECO:0000255|HAMAP-Rule:MF_00731,
CC ECO:0000269|PubMed:8626063}.
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:0000255|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:0000255|HAMAP-Rule:MF_00731}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00731}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC MenE subfamily. {ECO:0000255|HAMAP-Rule:MF_00731, ECO:0000305}.
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DR EMBL; L35031; AAB04893.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75320.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16084.1; -; Genomic_DNA.
DR PIR; B64997; B64997.
DR RefSeq; NP_416763.1; NC_000913.3.
DR RefSeq; WP_000577625.1; NZ_LN832404.1.
DR PDB; 5C5H; X-ray; 2.40 A; A/B=1-451.
DR PDB; 6NJ0; X-ray; 1.83 A; A=1-451.
DR PDBsum; 5C5H; -.
DR PDBsum; 6NJ0; -.
DR AlphaFoldDB; P37353; -.
DR SMR; P37353; -.
DR BioGRID; 4262001; 15.
DR DIP; DIP-10186N; -.
DR IntAct; P37353; 4.
DR STRING; 511145.b2260; -.
DR PaxDb; P37353; -.
DR PRIDE; P37353; -.
DR EnsemblBacteria; AAC75320; AAC75320; b2260.
DR EnsemblBacteria; BAA16084; BAA16084; BAA16084.
DR GeneID; 946741; -.
DR KEGG; ecj:JW2255; -.
DR KEGG; eco:b2260; -.
DR PATRIC; fig|1411691.4.peg.4476; -.
DR EchoBASE; EB2332; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_6; -.
DR InParanoid; P37353; -.
DR OMA; PIAYYPL; -.
DR PhylomeDB; P37353; -.
DR BioCyc; EcoCyc:O-SUCCINYLBENZOATE-COA-LIG-MON; -.
DR BioCyc; MetaCyc:O-SUCCINYLBENZOATE-COA-LIG-MON; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR PRO; PR:P37353; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0008756; F:o-succinylbenzoate-CoA ligase activity; IDA:EcoliWiki.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IMP:EcoCyc.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR010192; MenE.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR01923; menE; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Menaquinone biosynthesis;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..451
FT /note="2-succinylbenzoate--CoA ligase"
FT /id="PRO_0000193175"
FT CONFLICT 382
FT /note="I -> N (in Ref. 1; AAB04893)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:5C5H"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 30..46
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:6NJ0"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 332..341
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 364..372
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 377..387
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 391..403
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:6NJ0"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:6NJ0"
FT HELIX 440..448
FT /evidence="ECO:0007829|PDB:6NJ0"
SQ SEQUENCE 451 AA; 50185 MW; 2009B8092984EFB2 CRC64;
MIFSDWPWRH WRQVRGETIA LRLNDEQLNW RELCARVDEL ASGFAVQGVV EGSGVMLRAW
NTPQTLLAWL ALLQCGARVL PVNPQLPQPL LEELLPNLTL QFALVPDGEN TFPALTSLHI
QLVEGAHAAT WQPTRLCSMT LTSGSTGLPK AAVHTYQAHL ASAQGVLSLI PFGDHDDWLL
SLPLFHVSGQ GIMWRWLYAG ARMTVRDKQP LEQMLAGCTH ASLVPTQLWR LLVNRSSVSL
KAVLLGGAAI PVELTEQARE QGIRCFCGYG LTEFASTVCA KEADGLADVG SPLPGREVKI
VNNEVWLRAA SMAEGYWRNG QLVSLVNDEG WYATRDRGEM HNGKLTIVGR LDNLFFSGGE
GIQPEEVERV IAAHPAVLQV FIVPVADKEF GHRPVAVMEY DHESVDLSEW VKDKLARFQQ
PVRWLTLPPE LKNGGIKISR QALKEWVQRQ Q
