Q9F4L3 (Q9F4L3_PSEFL) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Benzaldehyde lyase EMBL AAG02282.1

Gene names

Name:

bznB EMBL AAG02282.1

Organism

Pseudomonas fluorescens EMBL AAG02282.1

Taxonomic identifier

294 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas fluorescens group

Protein attributes

Sequence length	563 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the TPP enzyme family. RuleBase RU003702

Ontologies

Keywords
Ligand	Calcium PDB 3IAE PDB 3D7K Magnesium PDB 2AG0 PDB 2AG1 PDB 3IAF Metal-binding PDB 2AG0 PDB 2AG1 PDB 3IAF PDB 3IAE PDB 3D7K Thiamine pyrophosphate PDB 2AG0 PDB 2AG1 PDB 2UZ1 PDB 3IAF
Molecular function	Lyase EMBL AAG02282.1
Technical term	3D-structure PDB 2AG0 PDB 2AG1 PDB 2UZ1 PDB 3IAF PDB 3IAE PDB 3D7K
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC
Molecular_function	lyase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Region	393 – 396	4	Thiamine pyrophosphate 1 binding PDB 2AG0 PDB 2AG1 PDB 2UZ1 PDB 3IAF
	Region	393 – 396	4	Thiamine pyrophosphate 2 binding PDB 3IAF
	Region	419 – 421	3	Thiamine pyrophosphate 1 binding PDB 2AG0 PDB 2AG1 PDB 2UZ1 PDB 3IAF
	Region	419 – 421	3	Thiamine pyrophosphate 2 binding PDB 3IAF
	Region	448 – 453	6	Thiamine pyrophosphate 1 binding PDB 2AG0 PDB 2AG1 PDB 2UZ1 PDB 3IAF
	Region	448 – 453	6	Thiamine pyrophosphate 2 binding PDB 3IAF
	Region	475 – 480	6	Thiamine pyrophosphate 1 binding PDB 2AG0 PDB 2AG1 PDB 2UZ1 PDB 3IAF
	Region	475 – 480	6	Thiamine pyrophosphate 2 binding PDB 3IAF
Sites
	Active site	29	1	Proton donor/acceptor PDB 2AG0
	Metal binding	448	1	Calcium 1 PDB 3IAE
	Metal binding	448	1	Calcium 2 PDB 3D7K
	Metal binding	448	1	Magnesium PDB 2AG0 PDB 2AG1 PDB 3IAF
	Metal binding	473	1	Calcium 1; via carbonyl oxygen PDB 3IAE
	Metal binding	475	1	Calcium 1 PDB 3IAE
	Metal binding	475	1	Calcium 2 PDB 3D7K
	Metal binding	475	1	Magnesium PDB 2AG0 PDB 2AG1 PDB 3IAF
	Metal binding	477	1	Calcium 2; via carbonyl oxygen PDB 3D7K
	Metal binding	477	1	Magnesium; via carbonyl oxygen PDB 2AG0 PDB 2AG1 PDB 3IAF
	Binding site	26	1	Thiamine pyrophosphate 4; via carbonyl oxygen PDB 2AG0
	Binding site	50	1	Thiamine pyrophosphate 1 PDB 3IAF
	Binding site	50	1	Thiamine pyrophosphate 2 PDB 3IAF
	Binding site	50	1	Thiamine pyrophosphate 3 PDB 2AG0 PDB 2AG1 PDB 2UZ1
	Binding site	50	1	Thiamine pyrophosphate 4 PDB 2AG0
	Binding site	50	1	Thiamine pyrophosphate 5 PDB 2AG0
	Binding site	76	1	Thiamine pyrophosphate 1 PDB 3IAF
	Binding site	76	1	Thiamine pyrophosphate 2 PDB 3IAF
	Binding site	76	1	Thiamine pyrophosphate 3 PDB 2AG0 PDB 2UZ1
	Binding site	113	1	Thiamine pyrophosphate 3 PDB 2AG1
	Site	50	1	Important for catalytic activity PDB 2AG0
	Site	113	1	Transition state stabilizer PDB 2AG0
	Site	419	1	Important for catalytic activity PDB 2AG0

Sequences

	Sequence		Length	Mass (Da)
	Q9F4L3 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 6511A404C501D126	FASTA	563	58,919
	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

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, 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY007242 Genomic DNA. Translation: AAG02282.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9F4L3.

SMR

Q9F4L3. Positions 2-555.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

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Family and domain databases

InterPro

IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]

Pfam

PF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q9F4L3.

Entry information

Entry name

Q9F4L3_PSEFL

Accession

Primary (citable) accession number: Q9F4L3

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2001
Last sequence update:	March 1, 2001
Last modified:	September 5, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)