Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Benzaldehyde lyase

Gene

bznB

Organism
Pseudomonas fluorescens
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

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

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

CalciumCombined sources, MagnesiumCombined sources, Metal-bindingCombined sources

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:
PDBei
RCSB PDBi
PDBji
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 bindingCombined sources
Regioni393 – 3964Thiaminepyrophosphate 2 bindingCombined sources
Regioni419 – 4213Thiaminepyrophosphate 1 bindingCombined sources
Regioni419 – 4213Thiaminepyrophosphate 2 bindingCombined sources
Regioni448 – 4536Thiaminepyrophosphate 1 bindingCombined sources
Regioni448 – 4536Thiaminepyrophosphate 2 bindingCombined sources
Regioni475 – 4806Thiaminepyrophosphate 1 bindingCombined sources
Regioni475 – 4806Thiaminepyrophosphate 2 bindingCombined sources

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

        10         20         30         40         50
MAMITGGELV VRTLIKAGVE HLFGLHGAHI DTIFQACLDH DVPIIDTRHE
60 70 80 90 100
AAAGHAAEGY ARAGAKLGVA LVTAGGGFTN AVTPIANAWL DRTPVLFLTG
110 120 130 140 150
SGALRDDETN TLQAGIDQVA MAAPITKWAH RVMATEHIPR LVMQAIRAAL
160 170 180 190 200
SAPRGPVLLD LPWDILMNQI DEDSVIIPDL VLSAHGARPD PADLDQALAL
210 220 230 240 250
LRKAERPVIV LGSEASRTAR KTALSAFVAA TGVPVFADYE GLSMLSGLPD
260 270 280 290 300
AMRGGLVQNL YSFAKADAAP DLVLMLGARF GLNTGHGSGQ LIPHSAQVIQ
310 320 330 340 350
VDPDACELGR LQGIALGIVA DVGGTIEALA QATAQDAAWP DRGDWCAKVT
360 370 380 390 400
DLAQERYASI AAKSSSEHAL HPFHASQVIA KHVDAGVTVV ADGALTYLWL
410 420 430 440 450
SEVMSRVKPG GFLCHGYLGS MGVGFGTALG AQVADLEAGR RTILVTGDGS
460 470 480 490 500
VGYSIGEFDT LVRKQLPLIV IIMNNQSWGA TLHFQQLAVG PNRVTGTRLE
510 520 530 540 550
NGSYHGVAAA FGADGYHVDS VESFSAALAQ ALAHNRPACI NVAVALDPIP
560
PEELILIGMD PFA
Length:563
Mass (Da):58,919
Last modified:March 1, 2001 - v1
Checksum:i6511A404C501D126
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007242 Genomic DNA. Translation: AAG02282.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007242 Genomic DNA. Translation: AAG02282.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F4L3.

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.
ProtoNetiSearch...

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: January 7, 2015
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.