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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)DescriptionActionsGraphical viewLength
Binding sitei26Thiamine pyrophosphate 1; via carbonyl oxygenCombined sources1
Binding sitei26Thiamine pyrophosphate 2; via carbonyl oxygenCombined sources1
Binding sitei26Thiamine pyrophosphate 4; via carbonyl oxygenCombined sources1
Active sitei29Proton donor/acceptorCombined sources1
Binding sitei50Thiamine pyrophosphate 1Combined sources1
Binding sitei50Thiamine pyrophosphate 2Combined sources1
Binding sitei50Thiamine pyrophosphate 3Combined sources1
Binding sitei50Thiamine pyrophosphate 4Combined sources1
Binding sitei50Thiamine pyrophosphate 5Combined sources1
Sitei50Important for catalytic activityCombined sources1
Binding sitei76Thiamine pyrophosphate 1Combined sources1
Binding sitei76Thiamine pyrophosphate 2Combined sources1
Binding sitei76Thiamine pyrophosphate 3Combined sources1
Binding sitei113Thiamine pyrophosphate 1Combined sources1
Binding sitei113Thiamine pyrophosphate 2Combined sources1
Binding sitei113Thiamine pyrophosphate 3Combined sources1
Sitei113Transition state stabilizerCombined sources1
Sitei419Important for catalytic activityCombined sources1
Metal bindingi448Calcium 1Combined sources1
Metal bindingi448Calcium 2Combined sources1
Metal bindingi448MagnesiumCombined sources1
Metal bindingi473Calcium 1; via carbonyl oxygenCombined sources1
Metal bindingi475Calcium 1Combined sources1
Metal bindingi475Calcium 2Combined sources1
Metal bindingi475MagnesiumCombined sources1
Metal bindingi477Calcium 2; via carbonyl oxygenCombined sources1
Metal bindingi477Magnesium; via carbonyl oxygenCombined sources1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

LyaseImported

Keywords - Ligandi

CalciumCombined sources, MagnesiumCombined sources, Metal-bindingCombined sources, Thiamine pyrophosphateUniRule annotationCombined 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
PDB 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[»]
4QPZX-ray3.00A/B/C/D/E/F/G/H2-563[»]
4QQ8X-ray2.88A/B/C/D1-563[»]
ProteinModelPortaliQ9F4L3.
SMRiQ9F4L3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F4L3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 173TPP_enzyme_NInterPro annotationAdd BLAST169
Domaini194 – 329TPP_enzyme_MInterPro annotationAdd BLAST136
Domaini397 – 542TPP_enzyme_CInterPro annotationAdd BLAST146

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni393 – 396Thiamine pyrophosphate 1 bindingCombined sources4
Regioni393 – 396Thiamine pyrophosphate 2 bindingCombined sources4
Regioni419 – 421Thiamine pyrophosphate 1 bindingCombined sources3
Regioni419 – 421Thiamine pyrophosphate 2 bindingCombined sources3
Regioni448 – 453Thiamine pyrophosphate 1 bindingCombined sources6
Regioni448 – 453Thiamine pyrophosphate 2 bindingCombined sources6
Regioni475 – 480Thiamine pyrophosphate 1 bindingCombined sources6
Regioni475 – 480Thiamine pyrophosphate 2 bindingCombined sources6

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
PDB 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[»]
4QPZX-ray3.00A/B/C/D/E/F/G/H2-563[»]
4QQ8X-ray2.88A/B/C/D1-563[»]
ProteinModelPortaliQ9F4L3.
SMRiQ9F4L3.
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...

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: November 2, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.