Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9F4L3

- Q9F4L3_PSEFL

UniProt

Q9F4L3 - Q9F4L3_PSEFL

Protein
Submitted name:

Benzaldehyde lyase

Gene

bznB

Organism
Pseudomonas fluorescens
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei26 – 261Thiaminepyrophosphate 4; via carbonyl oxygenImported
    Active sitei29 – 291Proton donor/acceptorImported
    Binding sitei50 – 501Thiaminepyrophosphate 1Imported
    Binding sitei50 – 501Thiaminepyrophosphate 2Imported
    Binding sitei50 – 501Thiaminepyrophosphate 3Imported
    Binding sitei50 – 501Thiaminepyrophosphate 4Imported
    Binding sitei50 – 501Thiaminepyrophosphate 5Imported
    Sitei50 – 501Important for catalytic activityImported
    Binding sitei76 – 761Thiaminepyrophosphate 1Imported
    Binding sitei76 – 761Thiaminepyrophosphate 2Imported
    Binding sitei76 – 761Thiaminepyrophosphate 3Imported
    Binding sitei113 – 1131Thiaminepyrophosphate 3Imported
    Sitei113 – 1131Transition state stabilizerImported
    Sitei419 – 4191Important for catalytic activityImported
    Metal bindingi448 – 4481Calcium 1Imported
    Metal bindingi448 – 4481Calcium 2Imported
    Metal bindingi448 – 4481Magnesium
    Metal bindingi473 – 4731Calcium 1; via carbonyl oxygenImported
    Metal bindingi475 – 4751Calcium 1Imported
    Metal bindingi475 – 4751Calcium 2Imported
    Metal bindingi475 – 4751Magnesium
    Metal bindingi477 – 4771Calcium 2; via carbonyl oxygenImported
    Metal bindingi477 – 4771Magnesium; via carbonyl oxygen

    GO - Molecular functioni

    1. lyase activity Source: UniProtKB-KW
    2. magnesium ion binding Source: InterPro
    3. thiamine pyrophosphate binding Source: InterPro

    Keywords - Molecular functioni

    LyaseImported

    Keywords - Ligandi

    CalciumImported, MagnesiumImported, Metal-bindingImported

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Benzaldehyde lyaseImported
    Gene namesi
    Name:bznBImported
    OrganismiPseudomonas fluorescensImported
    Taxonomic identifieri294 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AG0X-ray2.58A/B/C/D1-563[»]
    2AG1X-ray2.58A/B/C/D1-563[»]
    2UZ1X-ray1.65A/B/C/D1-563[»]
    3D7KX-ray2.49A/B1-562[»]
    3IAEX-ray2.30A/B1-562[»]
    3IAFX-ray2.80A/B/C/D1-562[»]
    ProteinModelPortaliQ9F4L3.
    SMRiQ9F4L3. Positions 2-555.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9F4L3.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni393 – 3964Thiaminepyrophosphate 1 bindingImported
    Regioni393 – 3964Thiaminepyrophosphate 2 bindingImported
    Regioni419 – 4213Thiaminepyrophosphate 1 bindingImported
    Regioni419 – 4213Thiaminepyrophosphate 2 bindingImported
    Regioni448 – 4536Thiaminepyrophosphate 1 bindingImported
    Regioni448 – 4536Thiaminepyrophosphate 2 bindingImported
    Regioni475 – 4806Thiaminepyrophosphate 1 bindingImported
    Regioni475 – 4806Thiaminepyrophosphate 2 bindingImported

    Sequence similaritiesi

    Belongs to the TPP enzyme family.UniRule annotation

    Family and domain databases

    Gene3Di3.40.50.1220. 1 hit.
    3.40.50.970. 2 hits.
    InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR029061. THDP-binding.
    IPR012000. Thiamin_PyroP_enz_cen_dom.
    IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
    IPR011766. TPP_enzyme-bd_C.
    [Graphical view]
    PfamiPF02775. TPP_enzyme_C. 1 hit.
    PF00205. TPP_enzyme_M. 1 hit.
    PF02776. TPP_enzyme_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF52467. SSF52467. 1 hit.
    SSF52518. SSF52518. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q9F4L3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMITGGELV VRTLIKAGVE HLFGLHGAHI DTIFQACLDH DVPIIDTRHE    50
    AAAGHAAEGY ARAGAKLGVA LVTAGGGFTN AVTPIANAWL DRTPVLFLTG 100
    SGALRDDETN TLQAGIDQVA MAAPITKWAH RVMATEHIPR LVMQAIRAAL 150
    SAPRGPVLLD LPWDILMNQI DEDSVIIPDL VLSAHGARPD PADLDQALAL 200
    LRKAERPVIV LGSEASRTAR KTALSAFVAA TGVPVFADYE GLSMLSGLPD 250
    AMRGGLVQNL YSFAKADAAP DLVLMLGARF GLNTGHGSGQ LIPHSAQVIQ 300
    VDPDACELGR LQGIALGIVA DVGGTIEALA QATAQDAAWP DRGDWCAKVT 350
    DLAQERYASI AAKSSSEHAL HPFHASQVIA KHVDAGVTVV ADGALTYLWL 400
    SEVMSRVKPG GFLCHGYLGS MGVGFGTALG AQVADLEAGR RTILVTGDGS 450
    VGYSIGEFDT LVRKQLPLIV IIMNNQSWGA TLHFQQLAVG PNRVTGTRLE 500
    NGSYHGVAAA FGADGYHVDS VESFSAALAQ ALAHNRPACI NVAVALDPIP 550
    PEELILIGMD PFA 563
    Length:563
    Mass (Da):58,919
    Last modified:March 1, 2001 - v1
    Checksum:i6511A404C501D126
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY007242 Genomic DNA. Translation: AAG02282.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY007242 Genomic DNA. Translation: AAG02282.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AG0 X-ray 2.58 A/B/C/D 1-563 [» ]
    2AG1 X-ray 2.58 A/B/C/D 1-563 [» ]
    2UZ1 X-ray 1.65 A/B/C/D 1-563 [» ]
    3D7K X-ray 2.49 A/B 1-562 [» ]
    3IAE X-ray 2.30 A/B 1-562 [» ]
    3IAF X-ray 2.80 A/B/C/D 1-562 [» ]
    ProteinModelPortali Q9F4L3.
    SMRi Q9F4L3. Positions 2-555.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q9F4L3.

    Family and domain databases

    Gene3Di 3.40.50.1220. 1 hit.
    3.40.50.970. 2 hits.
    InterProi IPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR029061. THDP-binding.
    IPR012000. Thiamin_PyroP_enz_cen_dom.
    IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
    IPR011766. TPP_enzyme-bd_C.
    [Graphical view ]
    Pfami PF02775. TPP_enzyme_C. 1 hit.
    PF00205. TPP_enzyme_M. 1 hit.
    PF02776. TPP_enzyme_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52467. SSF52467. 1 hit.
    SSF52518. SSF52518. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. Janzen E., Pohl M.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens."
      Mosbacher T.G., Mueller M., Schulz G.E.
      FEBS J. 272:6067-6076(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND THIAMINEPYROPHOSPHATE, ACTIVE SITE.
    3. "Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 A resolution."
      Maraite A., Schmidt T., Ansorge-Schumacher M.B., Brzozowski A.M., Grogan G.
      Acta Crystallogr. F 63:546-548(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH THIAMINEPYROPHOSPHATE.
    4. "Probing the active center of benzaldehyde lyase with substitutions and the pseudosubstrate analogue benzoylphosphonic acid methyl ester."
      Brandt G.S., Nemeria N., Chakraborty S., McLeish M.J., Yep A., Kenyon G.L., Petsko G.A., Jordan F., Ringe D.
      Biochemistry 47:7734-7743(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-562 IN COMPLEX WITH CALCIUM.
    5. "Active-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition."
      Brandt G.S., Kneen M.M., Petsko G.A., Ringe D., McLeish M.J.
      J. Am. Chem. Soc. 132:438-439(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-562 IN COMPLEX WITH CALCIUM; MAGNESIUM AND THIAMINEPYROPHOSPHATE.

    Entry informationi

    Entry nameiQ9F4L3_PSEFL
    AccessioniPrimary (citable) accession number: Q9F4L3
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 1, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported

    External Data

    Dasty 3