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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)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

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc: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)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

    STRINGi198094.BA_1986.

    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

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3DX5X-ray2.12A1-280[»]
    ProteinModelPortaliQ81RQ4.
    SMRiQ81RQ4.
    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.
    OMAiCTITFRH.

    Enzyme and pathway databases

    UniPathwayiUPA00088; UER00179.
    UPA01005.
    BioCyciMetaCyc: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...

    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: November 2, 2016
    This is version 84 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.