MENE_BACSU
ID MENE_BACSU Reviewed; 486 AA.
AC P23971; O34837;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
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}; OrderedLocusNames=BSU30790;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / RB1;
RX PubMed=1629163; DOI=10.1128/jb.174.15.5063-5071.1992;
RA Driscoll J.R., Taber H.W.;
RT "Sequence organization and regulation of the Bacillus subtilis menBE
RT operon.";
RL J. Bacteriol. 174:5063-5071(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / RB1;
RX PubMed=8566759; DOI=10.1016/0378-1119(95)00662-1;
RA Rowland B., Hill K., Miller P., Driscoll J.R., Taber H.W.;
RT "Structural organization of a Bacillus subtilis operon encoding menaquinone
RT biosynthetic enzymes.";
RL Gene 167:105-109(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA
CC (OSB-CoA). {ECO:0000255|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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50402.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC37017.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M74521; AAA50402.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M74538; AAC37017.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF008220; AAC00227.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15057.1; -; Genomic_DNA.
DR PIR; H69656; H69656.
DR RefSeq; NP_390957.1; NC_000964.3.
DR RefSeq; WP_003229056.1; NZ_JNCM01000036.1.
DR PDB; 5BUQ; X-ray; 1.98 A; A/B=1-486.
DR PDB; 5BUR; X-ray; 2.82 A; A/B=1-486.
DR PDB; 5BUS; X-ray; 2.60 A; A/B=1-486.
DR PDB; 5GTD; X-ray; 2.69 A; A/B=1-486.
DR PDB; 5X8F; X-ray; 1.76 A; A/B/C/D=2-486.
DR PDB; 5X8G; X-ray; 1.90 A; A/B/C/D=2-486.
DR PDBsum; 5BUQ; -.
DR PDBsum; 5BUR; -.
DR PDBsum; 5BUS; -.
DR PDBsum; 5GTD; -.
DR PDBsum; 5X8F; -.
DR PDBsum; 5X8G; -.
DR AlphaFoldDB; P23971; -.
DR SMR; P23971; -.
DR STRING; 224308.BSU30790; -.
DR PaxDb; P23971; -.
DR PRIDE; P23971; -.
DR EnsemblBacteria; CAB15057; CAB15057; BSU_30790.
DR GeneID; 937132; -.
DR KEGG; bsu:BSU30790; -.
DR PATRIC; fig|224308.179.peg.3337; -.
DR eggNOG; COG0318; Bacteria.
DR InParanoid; P23971; -.
DR OMA; WLMQRAF; -.
DR PhylomeDB; P23971; -.
DR BioCyc; BSUB:BSU30790-MON; -.
DR BioCyc; MetaCyc:MON-13811; -.
DR BRENDA; 6.2.1.26; 658.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
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 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..486
FT /note="2-succinylbenzoate--CoA ligase"
FT /id="PRO_0000193159"
FT CONFLICT 174..180
FT /note="VSSALNL -> CRPLLF (in Ref. 1; AAA50402 and 2;
FT AAC37017)"
FT /evidence="ECO:0000305"
FT CONFLICT 187..195
FT /note="RWLIALPLF -> AGLCIAAL (in Ref. 1; AAA50402 and 2;
FT AAC37017)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 8..15
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 31..47
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:5X8F"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:5BUS"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:5X8F"
FT TURN 303..308
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 351..357
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:5BUR"
FT STRAND 362..371
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:5BUQ"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 396..405
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 409..419
FT /evidence="ECO:0007829|PDB:5X8F"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 423..434
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 438..446
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:5X8F"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:5X8F"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:5BUQ"
SQ SEQUENCE 486 AA; 54190 MW; E0C062DFB10951FC CRC64;
MLTEQPNWLM QRAQLTPERI ALIYEDQTVT FAELFAASKR MAEQLAAHSV RKGDTAAILL
QNRAEMVYAV HACFLLGVKA VLLNTKLSTH ERLFQLEDSG SGFLLTDSSF EKKEYEHIVQ
TIDVDELMKE AAEEIEIEAY MQMDATATLM YTSGTTGKPK GVQQTFGNHY FSAVSSALNL
GITEQDRWLI ALPLFHISGL SALFKSVIYG MTVVLHQRFS VSDVLHSINR HEVTMISAVQ
TMLASLLEET NRCPESIRCI LLGGGPAPLP LLEECREKGF PVFQSYGMTE TCSQIVTLSP
EFSMEKLGSA GKPLFSCEIK IERDGQVCEP YEHGEIMVKG PNVMKSYFNR ESANEASFQN
GWLKTGDLGY LDNEGFLYVL DRRSDLIISG GENIYPAEVE SVLLSHPAVA EAGVSGAEDK
KWGKVPHAYL VLHKPVSAGE LTDYCKERLA KYKIPAKFFV LDRLPRNASN KLLRNQLKDA
RKGELL
