ID   DHBE_BACSU              Reviewed;         539 AA.
AC   P40871;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=2,3-dihydroxybenzoate-AMP ligase {ECO:0000303|PubMed:8921902};
DE            EC=6.2.1.71 {ECO:0000250|UniProtKB:P10378};
DE   AltName: Full=Dihydroxybenzoic acid-activating enzyme;
GN   Name=dhbE {ECO:0000303|PubMed:8921902}; Synonyms=entE;
GN   OrderedLocusNames=BSU31980;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=8921902; DOI=10.1016/0378-1119(96)00349-6;
RA   Rowland B.M., Grossman T.H., Osburne M.S., Taber H.W.;
RT   "Sequence and genetic organization of a Bacillus subtilis operon encoding
RT   2,3-dihydroxybenzoate biosynthetic enzymes.";
RL   Gene 178:119-123(1996).
RN   [2]
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 341-533.
RC   STRAIN=168;
RX   PubMed=8224884; DOI=10.1016/0378-1119(93)90235-u;
RA   Adams R., Schumann W.;
RT   "Cloning and mapping of the Bacillus subtilis locus homologous to
RT   Escherichia coli ent genes.";
RL   Gene 133:119-121(1993).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEXES WITH AMP AND
RP   2,3-DIHYDROXYBENZOATE.
RX   PubMed=12221282; DOI=10.1073/pnas.182156699;
RA   May J.J., Kessler N., Marahiel M.A., Stubbs M.T.;
RT   "Crystal structure of DhbE, an archetype for aryl acid activating domains
RT   of modular nonribosomal peptide synthetases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12120-12125(2002).
CC   -!- FUNCTION: Involved in the biosynthesis of the catecholic siderophore
CC       bacillibactin. Catalyzes the activation of the carboxylate group of
CC       2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions,
CC       to the acyladenylate. {ECO:0000269|PubMed:8921902}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-dihydroxybenzoate + ATP + holo-[ACP] = 2,3-
CC         dihydroxybenzoyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:61652,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:19024, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:36654, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:90610, ChEBI:CHEBI:456215; EC=6.2.1.71;
CC         Evidence={ECO:0000250|UniProtKB:P10378};
CC   -!- PATHWAY: Siderophore biosynthesis; bacillibactin biosynthesis.
CC       {ECO:0000305|PubMed:8921902}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; U26444; AAC44632.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15188.1; -; Genomic_DNA.
DR   EMBL; L08645; AAA79759.1; -; Genomic_DNA.
DR   PIR; D69615; D69615.
DR   RefSeq; NP_391078.1; NC_000964.3.
DR   RefSeq; WP_003243083.1; NZ_JNCM01000033.1.
DR   PDB; 1MD9; X-ray; 2.80 A; A=1-539.
DR   PDB; 1MDB; X-ray; 2.15 A; A=1-539.
DR   PDB; 1MDF; X-ray; 2.50 A; A=1-539.
DR   PDBsum; 1MD9; -.
DR   PDBsum; 1MDB; -.
DR   PDBsum; 1MDF; -.
DR   AlphaFoldDB; P40871; -.
DR   SMR; P40871; -.
DR   IntAct; P40871; 1.
DR   MINT; P40871; -.
DR   STRING; 224308.BSU31980; -.
DR   DrugBank; DB01672; 2,3-Dihydroxy-Benzoic Acid.
DR   jPOST; P40871; -.
DR   PaxDb; 224308-BSU31980; -.
DR   EnsemblBacteria; CAB15188; CAB15188; BSU_31980.
DR   GeneID; 936509; -.
DR   KEGG; bsu:BSU31980; -.
DR   PATRIC; fig|224308.179.peg.3464; -.
DR   eggNOG; COG1021; Bacteria.
DR   InParanoid; P40871; -.
DR   OrthoDB; 9757771at2; -.
DR   PhylomeDB; P40871; -.
DR   BioCyc; BSUB:BSU31980-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-13920; -.
DR   SABIO-RK; P40871; -.
DR   UniPathway; UPA00013; -.
DR   EvolutionaryTrace; P40871; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008668; F:(2,3-dihydroxybenzoyl)adenylate synthase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR   CDD; cd05920; 23DHB-AMP_lg; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
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; IPR011963; DHB_AMP_lig.
DR   NCBIfam; TIGR02275; DHB_AMP_lig; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..539
FT                   /note="2,3-dihydroxybenzoate-AMP ligase"
FT                   /id="PRO_0000193074"
FT   BINDING         191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:12221282"
FT   BINDING         234..235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:12221282"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:12221282"
FT   BINDING         307
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:12221282"
FT   BINDING         329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:12221282"
FT   BINDING         413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:12221282"
FT   BINDING         428
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:12221282"
FT   BINDING         519
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:12221282"
FT   BINDING         519
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:12221282"
FT   CONFLICT        360
FT                   /note="Y -> I (in Ref. 3; AAA79759)"
FT                   /evidence="ECO:0000305"
FT   HELIX           10..18
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           27..38
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           53..70
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:1MD9"
FT   HELIX           87..98
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          101..104
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           111..120
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          124..132
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           137..147
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          154..158
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          163..165
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           166..168
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          183..189
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          193..196
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          199..203
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           204..218
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          225..228
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           235..239
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           242..248
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          252..255
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          257..260
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           261..271
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          274..278
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           280..292
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          302..308
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           312..315
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           318..321
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          324..331
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          337..339
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          342..344
FT                   /evidence="ECO:0007829|PDB:1MDF"
FT   HELIX           346..351
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          355..358
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          362..366
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          379..384
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           396..402
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          409..417
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          419..421
FT                   /evidence="ECO:0007829|PDB:1MDF"
FT   STRAND          423..428
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           429..431
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          433..435
FT                   /evidence="ECO:0007829|PDB:1MDF"
FT   STRAND          438..440
FT                   /evidence="ECO:0007829|PDB:1MDF"
FT   HELIX           442..449
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          455..465
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   TURN            466..468
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          469..481
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           485..494
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           499..501
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   STRAND          504..508
FT                   /evidence="ECO:0007829|PDB:1MDB"
FT   HELIX           522..534
FT                   /evidence="ECO:0007829|PDB:1MDB"
SQ   SEQUENCE   539 AA;  59928 MW;  027D286940B192F8 CRC64;
     MLKGFTPWPD ELAETYRKNG CWAGETFGDL LRDRAAKYGD RIAITCGNTH WSYRELDTRA
     DRLAAGFQKL GIQQMDRVVV QLPNIKEFFE VIFALFRLGA LPVFALPSHR SSEITYFCEF
     AEAAAYIIPD AYSGFDYRSL ARQVQSKLPT LKNIIVAGEA EEFLPLEDLH AEPVKLPEVK
     SSDVAFLQLS GGSTGLSKLI PRTHDDYIYS LKRSVEVCWL DHSTVYLAAL PMAHNYPLSS
     PGVLGVLYAG GRVVLSPSPS PDDAFPLIER EKVTITALVP PLAMVWMDAA SSRRDDLSSL
     QVLQVGGAKF SAEAARRVKA VFGCTLQQVF GMAEGLVNYT RLDDPEEIIV NTQGKPMSPY
     DEMRVWDDHD RDVKPGETGH LLTRGPYTIR GYYKAEEHNA ASFTEDGFYR TGDIVRLTRD
     GYIVVEGRAK DQINRGGEKV AAEEVENHLL AHPAVHDAAM VSMPDQFLGE RSCVFIIPRD
     EAPKAAELKA FLRERGLAAY KIPDRVEFVE SFPQTGVGKV SKKALREAIS EKLLAGFKK
//