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Q9F4L3 (Q9F4L3_PSEFL) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein names
Gene names
Name:bznB EMBL AAG02282.1
OrganismPseudomonas fluorescens EMBL AAG02282.1
Taxonomic identifier294 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length563 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the TPP enzyme family. RuleBase RU003702

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region393 – 3964Thiamine pyrophosphate 1 binding
Region393 – 3964Thiamine pyrophosphate 2 binding
Region419 – 4213Thiamine pyrophosphate 1 binding
Region419 – 4213Thiamine pyrophosphate 2 binding
Region448 – 4536Thiamine pyrophosphate 1 binding
Region448 – 4536Thiamine pyrophosphate 2 binding
Region475 – 4806Thiamine pyrophosphate 1 binding
Region475 – 4806Thiamine pyrophosphate 2 binding

Sites

Active site291Proton donor/acceptor
Metal binding4481Calcium 1 PDB 3IAE
Metal binding4481Calcium 2 PDB 3D7K
Metal binding4481Magnesium
Metal binding4731Calcium 1; via carbonyl oxygen PDB 3IAE
Metal binding4751Calcium 1 PDB 3IAE
Metal binding4751Calcium 2 PDB 3D7K
Metal binding4751Magnesium
Metal binding4771Calcium 2; via carbonyl oxygen PDB 3D7K
Metal binding4771Magnesium; via carbonyl oxygen
Binding site261Thiamine pyrophosphate 4; via carbonyl oxygen PDB 2AG0
Binding site501Thiamine pyrophosphate 1
Binding site501Thiamine pyrophosphate 2
Binding site501Thiamine pyrophosphate 3 PDB 2AG0 PDB 2AG1
Binding site501Thiamine pyrophosphate 4 PDB 2AG0
Binding site501Thiamine pyrophosphate 5 PDB 2AG0
Binding site761Thiamine pyrophosphate 1
Binding site761Thiamine pyrophosphate 2
Binding site761Thiamine pyrophosphate 3 PDB 2AG0
Binding site1131Thiamine pyrophosphate 3 PDB 2AG1
Site501Important for catalytic activity
Site1131Transition state stabilizer
Site4191Important for catalytic activity

Sequences

Sequence LengthMass (Da)Tools
Q9F4L3 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 6511A404C501D126

FASTA56358,919
        10         20         30         40         50         60 
MAMITGGELV VRTLIKAGVE HLFGLHGAHI DTIFQACLDH DVPIIDTRHE AAAGHAAEGY 

        70         80         90        100        110        120 
ARAGAKLGVA LVTAGGGFTN AVTPIANAWL DRTPVLFLTG SGALRDDETN TLQAGIDQVA 

       130        140        150        160        170        180 
MAAPITKWAH RVMATEHIPR LVMQAIRAAL SAPRGPVLLD LPWDILMNQI DEDSVIIPDL 

       190        200        210        220        230        240 
VLSAHGARPD PADLDQALAL LRKAERPVIV LGSEASRTAR KTALSAFVAA TGVPVFADYE 

       250        260        270        280        290        300 
GLSMLSGLPD AMRGGLVQNL YSFAKADAAP DLVLMLGARF GLNTGHGSGQ LIPHSAQVIQ 

       310        320        330        340        350        360 
VDPDACELGR LQGIALGIVA DVGGTIEALA QATAQDAAWP DRGDWCAKVT DLAQERYASI 

       370        380        390        400        410        420 
AAKSSSEHAL HPFHASQVIA KHVDAGVTVV ADGALTYLWL SEVMSRVKPG GFLCHGYLGS 

       430        440        450        460        470        480 
MGVGFGTALG AQVADLEAGR RTILVTGDGS VGYSIGEFDT LVRKQLPLIV IIMNNQSWGA 

       490        500        510        520        530        540 
TLHFQQLAVG PNRVTGTRLE NGSYHGVAAA FGADGYHVDS VESFSAALAQ ALAHNRPACI 

       550        560 
NVAVALDPIP PEELILIGMD PFA 

« Hide

References

[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.
[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).
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY007242 Genomic DNA. Translation: AAG02282.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9F4L3.
SMRQ9F4L3. Positions 2-555.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9F4L3.

Entry information

Entry nameQ9F4L3_PSEFL
AccessionPrimary (citable) accession number: Q9F4L3
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)