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P40871

- DHBE_BACSU

UniProt

P40871 - DHBE_BACSU

Protein

2,3-dihydroxybenzoate-AMP ligase

Gene

dhbE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei240 – 2401Substrate
    Binding sitei329 – 3291ATP; via carbonyl oxygen
    Binding sitei413 – 4131ATP
    Binding sitei428 – 4281ATP
    Binding sitei519 – 5191ATP
    Binding sitei519 – 5191Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi191 – 1922ATP
    Nucleotide bindingi307 – 3093ATP

    GO - Molecular functioni

    1. (2,3-dihydroxybenzoyl)adenylate synthase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. ligase activity Source: UniProtKB-KW

    GO - Biological processi

    1. siderophore biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU31980-MONOMER.
    MetaCyc:MONOMER-13920.
    UniPathwayiUPA00013.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,3-dihydroxybenzoate-AMP ligase (EC:6.3.2.-)
    Alternative name(s):
    Dihydroxybenzoic acid-activating enzyme
    Gene namesi
    Name:dhbE
    Synonyms:entE
    Ordered Locus Names:BSU31980
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU31980. [Micado]

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5395392,3-dihydroxybenzoate-AMP ligasePRO_0000193074Add
    BLAST

    Proteomic databases

    PaxDbiP40871.

    Interactioni

    Protein-protein interaction databases

    IntActiP40871. 1 interaction.
    MINTiMINT-8366125.
    STRINGi224308.BSU31980.

    Structurei

    Secondary structure

    1
    539
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 189
    Helixi27 – 3812
    Beta strandi41 – 466
    Beta strandi49 – 524
    Helixi53 – 7018
    Beta strandi77 – 804
    Beta strandi84 – 863
    Helixi87 – 9812
    Beta strandi101 – 1044
    Helixi111 – 12010
    Beta strandi124 – 1329
    Helixi137 – 14711
    Beta strandi154 – 1585
    Beta strandi163 – 1653
    Helixi166 – 1683
    Beta strandi183 – 1897
    Beta strandi193 – 1964
    Beta strandi199 – 2035
    Helixi204 – 21815
    Beta strandi225 – 2284
    Helixi235 – 2395
    Helixi242 – 2487
    Beta strandi252 – 2554
    Beta strandi257 – 2604
    Helixi261 – 27111
    Beta strandi274 – 2785
    Helixi280 – 29213
    Beta strandi302 – 3087
    Helixi312 – 3154
    Helixi318 – 3214
    Beta strandi324 – 3318
    Beta strandi337 – 3393
    Beta strandi342 – 3443
    Helixi346 – 3516
    Beta strandi355 – 3584
    Beta strandi362 – 3665
    Beta strandi379 – 3846
    Helixi396 – 4027
    Beta strandi409 – 4179
    Beta strandi419 – 4213
    Beta strandi423 – 4286
    Helixi429 – 4313
    Beta strandi433 – 4353
    Beta strandi438 – 4403
    Helixi442 – 4498
    Beta strandi455 – 46511
    Turni466 – 4683
    Beta strandi469 – 48113
    Helixi485 – 49410
    Helixi499 – 5013
    Beta strandi504 – 5085
    Helixi522 – 53413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MD9X-ray2.80A1-539[»]
    1MDBX-ray2.15A1-539[»]
    1MDFX-ray2.50A1-539[»]
    ProteinModelPortaliP40871.
    SMRiP40871. Positions 1-536.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40871.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni234 – 2352Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1021.
    HOGENOMiHOG000230011.
    KOiK02363.
    OMAiMENELMG.
    OrthoDBiEOG600DJW.
    PhylomeDBiP40871.

    Family and domain databases

    InterProiIPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    IPR011963. DHB_AMP_lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02275. DHB_AMP_lig. 1 hit.
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P40871-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKGFTPWPD ELAETYRKNG CWAGETFGDL LRDRAAKYGD RIAITCGNTH    50
    WSYRELDTRA DRLAAGFQKL GIQQMDRVVV QLPNIKEFFE VIFALFRLGA 100
    LPVFALPSHR SSEITYFCEF AEAAAYIIPD AYSGFDYRSL ARQVQSKLPT 150
    LKNIIVAGEA EEFLPLEDLH AEPVKLPEVK SSDVAFLQLS GGSTGLSKLI 200
    PRTHDDYIYS LKRSVEVCWL DHSTVYLAAL PMAHNYPLSS PGVLGVLYAG 250
    GRVVLSPSPS PDDAFPLIER EKVTITALVP PLAMVWMDAA SSRRDDLSSL 300
    QVLQVGGAKF SAEAARRVKA VFGCTLQQVF GMAEGLVNYT RLDDPEEIIV 350
    NTQGKPMSPY DEMRVWDDHD RDVKPGETGH LLTRGPYTIR GYYKAEEHNA 400
    ASFTEDGFYR TGDIVRLTRD GYIVVEGRAK DQINRGGEKV AAEEVENHLL 450
    AHPAVHDAAM VSMPDQFLGE RSCVFIIPRD EAPKAAELKA FLRERGLAAY 500
    KIPDRVEFVE SFPQTGVGKV SKKALREAIS EKLLAGFKK 539
    Length:539
    Mass (Da):59,928
    Last modified:November 1, 1995 - v2
    Checksum:i027D286940B192F8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti360 – 3601Y → I in AAA79759. (PubMed:8224884)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26444 Genomic DNA. Translation: AAC44632.1.
    AL009126 Genomic DNA. Translation: CAB15188.1.
    L08645 Genomic DNA. Translation: AAA79759.1.
    PIRiD69615.
    RefSeqiNP_391078.1. NC_000964.3.
    WP_003243083.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB15188; CAB15188; BSU31980.
    GeneIDi936509.
    KEGGibsu:BSU31980.
    PATRICi18978368. VBIBacSub10457_3347.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26444 Genomic DNA. Translation: AAC44632.1 .
    AL009126 Genomic DNA. Translation: CAB15188.1 .
    L08645 Genomic DNA. Translation: AAA79759.1 .
    PIRi D69615.
    RefSeqi NP_391078.1. NC_000964.3.
    WP_003243083.1. NZ_CM000487.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MD9 X-ray 2.80 A 1-539 [» ]
    1MDB X-ray 2.15 A 1-539 [» ]
    1MDF X-ray 2.50 A 1-539 [» ]
    ProteinModelPortali P40871.
    SMRi P40871. Positions 1-536.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P40871. 1 interaction.
    MINTi MINT-8366125.
    STRINGi 224308.BSU31980.

    Proteomic databases

    PaxDbi P40871.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15188 ; CAB15188 ; BSU31980 .
    GeneIDi 936509.
    KEGGi bsu:BSU31980.
    PATRICi 18978368. VBIBacSub10457_3347.

    Organism-specific databases

    GenoListi BSU31980. [Micado ]

    Phylogenomic databases

    eggNOGi COG1021.
    HOGENOMi HOG000230011.
    KOi K02363.
    OMAi MENELMG.
    OrthoDBi EOG600DJW.
    PhylomeDBi P40871.

    Enzyme and pathway databases

    UniPathwayi UPA00013 .
    BioCyci BSUB:BSU31980-MONOMER.
    MetaCyc:MONOMER-13920.

    Miscellaneous databases

    EvolutionaryTracei P40871.

    Family and domain databases

    InterProi IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    IPR011963. DHB_AMP_lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02275. DHB_AMP_lig. 1 hit.
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiDHBE_BACSU
    AccessioniPrimary (citable) accession number: P40871
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3