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Protein

3-dehydroshikimate dehydratase

Gene

asbF

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts 3-dehydroshikimate to protocatechuate (3,4-dihydroxybenzoate), a biosynthetic unit required for the biosynthesis of petrobactin which is a virulence-associated siderophore produced by B.anthracis.1 Publication

Catalytic activityi

3-dehydro-shikimate = protocatechuate + H2O.1 Publication

Cofactori

Mn2+1 PublicationNote: Binds 1 Mn2+ ion per subunit.1 Publication

Kineticsi

  1. KM=290 µM for 3-dehydro-shikimate1 Publication

    pH dependencei

    Optimum pH is >9.5.1 Publication

    Pathwayi: 3,4-dihydroxybenzoate biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes 3,4-dihydroxybenzoate from 3-dehydroquinate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. 3-dehydroshikimate dehydratase (asbF)
    This subpathway is part of the pathway 3,4-dihydroxybenzoate biosynthesis, which is itself part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 3,4-dihydroxybenzoate from 3-dehydroquinate, the pathway 3,4-dihydroxybenzoate biosynthesis and in Aromatic compound metabolism.

    Pathwayi: petrobactin biosynthesis

    This protein is involved in the pathway petrobactin biosynthesis, which is part of Siderophore biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway petrobactin biosynthesis and in Siderophore biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei70 – 701Substrate1 Publication
    Binding sitei102 – 1021Substrate1 Publication
    Metal bindingi142 – 1421Manganese
    Binding sitei142 – 1421Substrate1 Publication
    Active sitei144 – 1441Proton acceptor
    Metal bindingi172 – 1721Manganese
    Binding sitei172 – 1721Substrate1 Publication
    Binding sitei175 – 1751Substrate1 Publication
    Metal bindingi198 – 1981Manganese
    Binding sitei217 – 2171Substrate1 Publication
    Metal bindingi253 – 2531Manganese
    Binding sitei253 – 2531Substrate1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciBANT260799:GJAJ-1912-MONOMER.
    BANT261594:GJ7F-1987-MONOMER.
    MetaCyc:MONOMER-14940.
    SABIO-RKQ81RQ4.
    UniPathwayiUPA00088; UER00179.
    UPA01005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-dehydroshikimate dehydratase (EC:4.2.1.118)
    Short name:
    3-DHS dehydratase
    Short name:
    DHSase
    Alternative name(s):
    Petrobactin biosynthesis protein AsbF
    Gene namesi
    Name:asbF
    Ordered Locus Names:BA_1986, GBAA_1986, BAS1843
    OrganismiBacillus anthracis
    Taxonomic identifieri1392 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    Proteomesi
    • UP000000594 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi70 – 701Y → A: Binds substrate with 10-fold lower affinity; when associagted with A-217. 1 Publication
    Mutagenesisi102 – 1021R → A: No activity. 1 Publication
    Mutagenesisi144 – 1441H → A: No activity. 1 Publication
    Mutagenesisi175 – 1751H → A: Only trace activity remaining. 1 Publication
    Mutagenesisi200 – 2001K → A or E: No activity. 1 Publication
    Mutagenesisi200 – 2001K → R: Less than 5% activity remaining. 1 Publication
    Mutagenesisi217 – 2171Y → A: Binds substrate with 10-fold lower affinity; when associagted with A-70. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2802803-dehydroshikimate dehydratasePRO_0000400088Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi198094.BA_1986.

    Structurei

    Secondary structure

    1
    280
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65Combined sources
    Helixi7 – 104Combined sources
    Helixi17 – 2610Combined sources
    Beta strandi31 – 355Combined sources
    Helixi36 – 4510Combined sources
    Helixi47 – 5610Combined sources
    Helixi58 – 603Combined sources
    Beta strandi64 – 685Combined sources
    Helixi79 – 9618Combined sources
    Beta strandi100 – 1034Combined sources
    Helixi110 – 1123Combined sources
    Helixi115 – 13420Combined sources
    Beta strandi138 – 1425Combined sources
    Helixi152 – 16211Combined sources
    Beta strandi167 – 1726Combined sources
    Helixi173 – 1786Combined sources
    Helixi183 – 1908Combined sources
    Helixi191 – 1933Combined sources
    Beta strandi194 – 1996Combined sources
    Beta strandi201 – 2033Combined sources
    Helixi205 – 2117Combined sources
    Helixi213 – 2175Combined sources
    Helixi229 – 2313Combined sources
    Beta strandi232 – 2343Combined sources
    Helixi236 – 2438Combined sources
    Beta strandi249 – 2524Combined sources
    Helixi259 – 27214Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DX5X-ray2.12A1-280[»]
    ProteinModelPortaliQ81RQ4.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ81RQ4.

    Family & Domainsi

    Phylogenomic databases

    eggNOGiENOG4108WBH. Bacteria.
    ENOG4111KIK. LUCA.
    HOGENOMiHOG000088353.
    KOiK15652.
    OMAiDGIELWG.
    OrthoDBiEOG6038VK.

    Family and domain databases

    Gene3Di3.20.20.150. 1 hit.
    InterProiIPR013022. Xyl_isomerase-like_TIM-brl.
    [Graphical view]
    PfamiPF01261. AP_endonuc_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51658. SSF51658. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q81RQ4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKYSLCTISF RHQLISFTDI VQFAYENGFE GIELWGTHAQ NLYMQEYETT
    60 70 80 90 100
    ERELNCLKDK TLEITMISDY LDISLSADFE KTIEKCEQLA ILANWFKTNK
    110 120 130 140 150
    IRTFAGQKGS ADFSQQERQE YVNRIRMICE LFAQHNMYVL LETHPNTLTD
    160 170 180 190 200
    TLPSTLELLG EVDHPNLKIN LDFLHIWESG ADPVDSFQQL RPWIQHYHFK
    210 220 230 240 250
    NISSADYLHV FEPNNVYAAA GNRTGMVPLF EGIVNYDEII QEVRDTDHFA
    260 270 280
    SLEWFGHNAK DILKAEMKVL TNRNLEVVTS
    Length:280
    Mass (Da):32,589
    Last modified:June 1, 2003 - v1
    Checksum:iEA349FA7BFDA4D98
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE016879 Genomic DNA. Translation: AAP25878.1.
    AE017334 Genomic DNA. Translation: AAT31105.1.
    AE017225 Genomic DNA. Translation: AAT54158.1.
    RefSeqiNP_844392.1. NC_003997.3.
    WP_000877695.1. NZ_LHUO01000023.1.
    YP_028107.1. NC_005945.1.

    Genome annotation databases

    EnsemblBacteriaiAAP25878; AAP25878; BA_1986.
    AAT31105; AAT31105; GBAA_1986.
    AAT54158; AAT54158; BAS1843.
    GeneIDi1085888.
    2848581.
    KEGGiban:BA_1986.
    bar:GBAA_1986.
    bat:BAS1843.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE016879 Genomic DNA. Translation: AAP25878.1.
    AE017334 Genomic DNA. Translation: AAT31105.1.
    AE017225 Genomic DNA. Translation: AAT54158.1.
    RefSeqiNP_844392.1. NC_003997.3.
    WP_000877695.1. NZ_LHUO01000023.1.
    YP_028107.1. NC_005945.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DX5X-ray2.12A1-280[»]
    ProteinModelPortaliQ81RQ4.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi198094.BA_1986.

    Protocols and materials databases

    DNASUi1085888.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAP25878; AAP25878; BA_1986.
    AAT31105; AAT31105; GBAA_1986.
    AAT54158; AAT54158; BAS1843.
    GeneIDi1085888.
    2848581.
    KEGGiban:BA_1986.
    bar:GBAA_1986.
    bat:BAS1843.

    Phylogenomic databases

    eggNOGiENOG4108WBH. Bacteria.
    ENOG4111KIK. LUCA.
    HOGENOMiHOG000088353.
    KOiK15652.
    OMAiDGIELWG.
    OrthoDBiEOG6038VK.

    Enzyme and pathway databases

    UniPathwayiUPA00088; UER00179.
    UPA01005.
    BioCyciBANT260799:GJAJ-1912-MONOMER.
    BANT261594:GJ7F-1987-MONOMER.
    MetaCyc:MONOMER-14940.
    SABIO-RKQ81RQ4.

    Miscellaneous databases

    EvolutionaryTraceiQ81RQ4.

    Family and domain databases

    Gene3Di3.20.20.150. 1 hit.
    InterProiIPR013022. Xyl_isomerase-like_TIM-brl.
    [Graphical view]
    PfamiPF01261. AP_endonuc_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51658. SSF51658. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
      Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
      , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
      Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames / isolate Porton.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames ancestor.
    3. "Complete genome sequence of Bacillus anthracis Sterne."
      Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Sterne.
    4. "Structural and functional analysis of AsbF: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis."
      Pfleger B.F., Kim Y., Nusca T.D., Maltseva N., Lee J.Y., Rath C.M., Scaglione J.B., Janes B.K., Anderson E.C., Bergman N.H., Hanna P.C., Joachimiak A., Sherman D.H.
      Proc. Natl. Acad. Sci. U.S.A. 105:17133-17138(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-70; ARG-102; HIS-144; HIS-175; LYS-200 AND TYR-217, REACTION MECHANISM.
      Strain: Sterne.

    Entry informationi

    Entry nameiASBF_BACAN
    AccessioniPrimary (citable) accession number: Q81RQ4
    Secondary accession number(s): Q6HZY1, Q6KTW0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2010
    Last sequence update: June 1, 2003
    Last modified: January 20, 2016
    This is version 82 of the entry and version 1 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.