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P40871 (DHBE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2,3-dihydroxybenzoate-AMP ligase

EC=6.3.2.-
Alternative name(s):
Dihydroxybenzoic acid-activating enzyme
Gene names
Name:dhbE
Synonyms:entE
Ordered Locus Names:BSU31980
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate.

Pathway

Siderophore biosynthesis; bacillibactin biosynthesis.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processsiderophore biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function(2,3-dihydroxybenzoyl)adenylate synthase activity

Inferred from electronic annotation. Source: InterPro

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5395392,3-dihydroxybenzoate-AMP ligase
PRO_0000193074

Regions

Nucleotide binding191 – 1922ATP
Nucleotide binding307 – 3093ATP
Region234 – 2352Substrate binding

Sites

Binding site2401Substrate
Binding site3291ATP; via carbonyl oxygen
Binding site4131ATP
Binding site4281ATP
Binding site5191ATP
Binding site5191Substrate

Experimental info

Sequence conflict3601Y → I in AAA79759. Ref.3

Secondary structure

................................................................................................. 539
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40871 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 027D286940B192F8

FASTA53959,928
        10         20         30         40         50         60 
MLKGFTPWPD ELAETYRKNG CWAGETFGDL LRDRAAKYGD RIAITCGNTH WSYRELDTRA 

        70         80         90        100        110        120 
DRLAAGFQKL GIQQMDRVVV QLPNIKEFFE VIFALFRLGA LPVFALPSHR SSEITYFCEF 

       130        140        150        160        170        180 
AEAAAYIIPD AYSGFDYRSL ARQVQSKLPT LKNIIVAGEA EEFLPLEDLH AEPVKLPEVK 

       190        200        210        220        230        240 
SSDVAFLQLS GGSTGLSKLI PRTHDDYIYS LKRSVEVCWL DHSTVYLAAL PMAHNYPLSS 

       250        260        270        280        290        300 
PGVLGVLYAG GRVVLSPSPS PDDAFPLIER EKVTITALVP PLAMVWMDAA SSRRDDLSSL 

       310        320        330        340        350        360 
QVLQVGGAKF SAEAARRVKA VFGCTLQQVF GMAEGLVNYT RLDDPEEIIV NTQGKPMSPY 

       370        380        390        400        410        420 
DEMRVWDDHD RDVKPGETGH LLTRGPYTIR GYYKAEEHNA ASFTEDGFYR TGDIVRLTRD 

       430        440        450        460        470        480 
GYIVVEGRAK DQINRGGEKV AAEEVENHLL AHPAVHDAAM VSMPDQFLGE RSCVFIIPRD 

       490        500        510        520        530 
EAPKAAELKA FLRERGLAAY KIPDRVEFVE SFPQTGVGKV SKKALREAIS EKLLAGFKK 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and genetic organization of a Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes."
Rowland B.M., Grossman T.H., Osburne M.S., Taber H.W.
Gene 178:119-123(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Cloning and mapping of the Bacillus subtilis locus homologous to Escherichia coli ent genes."
Adams R., Schumann W.
Gene 133:119-121(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 341-533.
Strain: 168.
[4]"Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases."
May J.J., Kessler N., Marahiel M.A., Stubbs M.T.
Proc. Natl. Acad. Sci. U.S.A. 99:12120-12125(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEXES WITH AMP AND 2,3-DIHYDROXYBENZOATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U26444 Genomic DNA. Translation: AAC44632.1.
AL009126 Genomic DNA. Translation: CAB15188.1.
L08645 Genomic DNA. Translation: AAA79759.1.
PIRD69615.
RefSeqNP_391078.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MD9X-ray2.80A1-539[»]
1MDBX-ray2.15A1-539[»]
1MDFX-ray2.50A1-539[»]
ProteinModelPortalP40871.
SMRP40871. Positions 1-536.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP40871. 1 interaction.
MINTMINT-8366125.
STRING224308.BSU31980.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

Proteomic databases

PaxDbP40871.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15188; CAB15188; BSU31980.
GeneID936509.
KEGGbsu:BSU31980.
PATRIC18978368. VBIBacSub10457_3347.

Organism-specific databases

GenoListBSU31980. [Micado]

Phylogenomic databases

eggNOGCOG1021.
HOGENOMHOG000230011.
KOK02363.
OMAILGERTC.
OrthoDBEOG600DJW.
ProtClustDBCLSK887818.

Enzyme and pathway databases

BioCycBSUB:BSU31980-MONOMER.
MetaCyc:MONOMER-13920.
UniPathwayUPA00013.

Family and domain databases

InterProIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR011963. DHB_AMP_lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02275. DHB_AMP_lig. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP40871.

Entry information

Entry nameDHBE_BACSU
AccessionPrimary (citable) accession number: P40871
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: December 11, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList