DHBE_BACSU
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 03-AUG-2022, entry version 140.
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; Firmicutes; 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 / NCIMB
RC 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-[aryl-carrier protein] =
CC 2,3-dihydroxybenzoyl-[aryl-carrier protein] + AMP + diphosphate;
CC Xref=Rhea:RHEA:61652, Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:17559,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:36654,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:90610, ChEBI:CHEBI:456215;
CC EC=6.2.1.71; 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; P40871; -.
DR PRIDE; P40871; -.
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 OMA; WHEAAVI; -.
DR PhylomeDB; P40871; -.
DR BioCyc; BSUB:BSU31980-MON; -.
DR BioCyc; MetaCyc:MON-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 Gene3D; 3.30.300.30; -; 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; IPR011963; DHB_AMP_lig.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02275; DHB_AMP_lig; 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
