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Protein

3-dehydroshikimate dehydratase

Gene

asbF

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
    Binding sitei70Substrate1 Publication1
    Binding sitei102Substrate1 Publication1
    Metal bindingi142Manganese1
    Binding sitei142Substrate1 Publication1
    Active sitei144Proton acceptor1
    Metal bindingi172Manganese1
    Binding sitei172Substrate1 Publication1
    Binding sitei175Substrate1 Publication1
    Metal bindingi198Manganese1
    Binding sitei217Substrate1 Publication1
    Metal bindingi253Manganese1
    Binding sitei253Substrate1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionLyase
    LigandManganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14940
    SABIO-RKiQ81RQ4
    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
    • UP000000427 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi70Y → A: Binds substrate with 10-fold lower affinity; when associagted with A-217. 1 Publication1
    Mutagenesisi102R → A: No activity. 1 Publication1
    Mutagenesisi144H → A: No activity. 1 Publication1
    Mutagenesisi175H → A: Only trace activity remaining. 1 Publication1
    Mutagenesisi200K → A or E: No activity. 1 Publication1
    Mutagenesisi200K → R: Less than 5% activity remaining. 1 Publication1
    Mutagenesisi217Y → A: Binds substrate with 10-fold lower affinity; when associagted with A-70. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004000881 – 2803-dehydroshikimate dehydrataseAdd BLAST280

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi260799.BAS1843

    Structurei

    Secondary structure

    1280
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 6Combined sources5
    Helixi7 – 10Combined sources4
    Helixi17 – 26Combined sources10
    Beta strandi31 – 35Combined sources5
    Helixi36 – 45Combined sources10
    Helixi47 – 56Combined sources10
    Helixi58 – 60Combined sources3
    Beta strandi64 – 68Combined sources5
    Helixi79 – 96Combined sources18
    Beta strandi100 – 103Combined sources4
    Helixi110 – 112Combined sources3
    Helixi115 – 134Combined sources20
    Beta strandi138 – 142Combined sources5
    Helixi152 – 162Combined sources11
    Beta strandi167 – 172Combined sources6
    Helixi173 – 178Combined sources6
    Helixi183 – 190Combined sources8
    Helixi191 – 193Combined sources3
    Beta strandi194 – 199Combined sources6
    Beta strandi201 – 203Combined sources3
    Helixi205 – 211Combined sources7
    Helixi213 – 217Combined sources5
    Helixi229 – 231Combined sources3
    Beta strandi232 – 234Combined sources3
    Helixi236 – 243Combined sources8
    Beta strandi249 – 252Combined sources4
    Helixi259 – 272Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3DX5X-ray2.12A1-280[»]
    ProteinModelPortaliQ81RQ4
    SMRiQ81RQ4
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ81RQ4

    Family & Domainsi

    Phylogenomic databases

    eggNOGiENOG4108WBH Bacteria
    ENOG4111KIK LUCA
    HOGENOMiHOG000088353
    KOiK15652
    OMAiCTITFRH

    Family and domain databases

    InterProiView protein in InterPro
    IPR036237 Xyl_isomerase-like_sf
    IPR013022 Xyl_isomerase-like_TIM-brl
    PfamiView protein in Pfam
    PF01261 AP_endonuc_2, 1 hit
    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_NRJB01000003.1
    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
    PATRICifig|198094.11.peg.1957

    Similar proteinsi

    Entry informationi

    Entry nameiASBF_BACAN
    AccessioniPrimary (citable) accession number: Q81RQ4
    Secondary accession number(s): Q6HZY1, Q6KTW0
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2010
    Last sequence update: June 1, 2003
    Last modified: April 25, 2018
    This is version 92 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
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    Main funding by: National Institutes of Health