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Q9F4L3

- Q9F4L3_PSEFL

UniProt

Q9F4L3 - Q9F4L3_PSEFL

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Protein
Submitted name: Benzaldehyde lyase
Gene
bznB
Organism
Pseudomonas fluorescens
Status
Unreviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

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

GO - Molecular functioni

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

Keywords - Molecular functioni

LyaseImported

Keywords - Ligandi

CalciumImported, MagnesiumImported, Metal-bindingImported, Thiamine pyrophosphateImported

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.

Miscellaneous databases

EvolutionaryTraceiQ9F4L3.

Family & Domainsi

Region

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

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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 THIAMINE PYROPHOSPHATE, 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 THIAMINE PYROPHOSPHATE.
  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 THIAMINE PYROPHOSPHATE.

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: June 11, 2014
This is version 56 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

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