ID Q9F4L3_PSEFL Unreviewed; 563 AA. AC Q9F4L3; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 01-OCT-2014, entry version 57. DE SubName: Full=Benzaldehyde lyase {ECO:0000313|EMBL:AAG02282.1}; GN Name=bznB {ECO:0000313|EMBL:AAG02282.1}; OS Pseudomonas fluorescens. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=294 {ECO:0000313|EMBL:AAG02282.1}; RN [1] {ECO:0000313|EMBL:AAG02282.1} RP NUCLEOTIDE SEQUENCE. RA Janzen E., Pohl M.; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|PDB:2AG0, ECO:0000313|PDB:2AG1} RP X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND RP THIAMINEPYROPHOSPHATE, AND ACTIVE SITE. RX PubMed=16302970; DOI=10.1111/j.1742-4658.2005.04998.x; RA Mosbacher T.G., Mueller M., Schulz G.E.; RT "Structure and mechanism of the ThDP-dependent benzaldehyde lyase from RT Pseudomonas fluorescens."; RL FEBS J. 272:6067-6076(2005). RN [3] {ECO:0000313|PDB:2UZ1} RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH RP THIAMINEPYROPHOSPHATE. RX PubMed=17620706; RA Maraite A., Schmidt T., Ansorge-Schumacher M.B., Brzozowski A.M., RA Grogan G.; RT "Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to RT 1.65 A resolution."; RL Acta Crystallogr. F 63:546-548(2007). RN [4] {ECO:0000313|PDB:3D7K} RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-562 IN COMPLEX WITH RP CALCIUM. RX PubMed=18570438; DOI=10.1021/bi8004413; RA Brandt G.S., Nemeria N., Chakraborty S., McLeish M.J., Yep A., RA Kenyon G.L., Petsko G.A., Jordan F., Ringe D.; RT "Probing the active center of benzaldehyde lyase with substitutions RT and the pseudosubstrate analogue benzoylphosphonic acid methyl RT ester."; RL Biochemistry 47:7734-7743(2008). RN [5] {ECO:0000313|PDB:3IAE, ECO:0000313|PDB:3IAF} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-562 IN COMPLEX WITH RP CALCIUM; MAGNESIUM AND THIAMINEPYROPHOSPHATE. RX PubMed=20030408; DOI=10.1021/ja907064w; RA Brandt G.S., Kneen M.M., Petsko G.A., Ringe D., McLeish M.J.; RT "Active-site engineering of benzaldehyde lyase shows that a point RT mutation can confer both new reactivity and susceptibility to RT mechanism-based inhibition."; RL J. Am. Chem. Soc. 132:438-439(2010). CC -!- SIMILARITY: Belongs to the TPP enzyme family. CC {ECO:0000256|RuleBase:RU003702}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY007242; AAG02282.1; -; Genomic_DNA. DR PDB; 2AG0; X-ray; 2.58 A; A/B/C/D=1-563. DR PDB; 2AG1; X-ray; 2.58 A; A/B/C/D=1-563. DR PDB; 2UZ1; X-ray; 1.65 A; A/B/C/D=1-563. DR PDB; 3D7K; X-ray; 2.49 A; A/B=1-562. DR PDB; 3IAE; X-ray; 2.30 A; A/B=1-562. DR PDB; 3IAF; X-ray; 2.80 A; A/B/C/D=1-562. DR PDBsum; 2AG0; -. DR PDBsum; 2AG1; -. DR PDBsum; 2UZ1; -. DR PDBsum; 3D7K; -. DR PDBsum; 3IAE; -. DR PDBsum; 3IAF; -. DR ProteinModelPortal; Q9F4L3; -. DR SMR; Q9F4L3; 2-555. DR EvolutionaryTrace; Q9F4L3; -. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR Gene3D; 3.40.50.1220; -; 1. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF00205; TPP_enzyme_M; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52467; SSF52467; 1. DR SUPFAM; SSF52518; SSF52518; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000313|PDB:2AG0, ECO:0000313|PDB:2AG1, KW ECO:0000313|PDB:2UZ1, ECO:0000313|PDB:3D7K, ECO:0000313|PDB:3IAE, KW ECO:0000313|PDB:3IAF}; KW Calcium {ECO:0000313|PDB:3D7K, ECO:0000313|PDB:3IAE}; KW Lyase {ECO:0000313|EMBL:AAG02282.1}; KW Magnesium {ECO:0000313|PDB:2AG0, ECO:0000313|PDB:2AG1, KW ECO:0000313|PDB:3IAF}; KW Metal-binding {ECO:0000313|PDB:2AG0, ECO:0000313|PDB:2AG1, KW ECO:0000313|PDB:3D7K, ECO:0000313|PDB:3IAE, ECO:0000313|PDB:3IAF}. FT REGION 393 396 Thiaminepyrophosphate 1 binding. {ECO: FT 0000313|PDB:2AG0, ECO:0000313|PDB:2AG1, FT ECO:0000313|PDB:2UZ1, ECO:0000313|PDB: FT 3IAF}. FT REGION 393 396 Thiaminepyrophosphate 2 binding. {ECO: FT 0000313|PDB:3IAF}. FT REGION 419 421 Thiaminepyrophosphate 1 binding. {ECO: FT 0000313|PDB:2AG0, ECO:0000313|PDB:2AG1, FT ECO:0000313|PDB:2UZ1, ECO:0000313|PDB: FT 3IAF}. FT REGION 419 421 Thiaminepyrophosphate 2 binding. {ECO: FT 0000313|PDB:3IAF}. FT REGION 448 453 Thiaminepyrophosphate 1 binding. {ECO: FT 0000313|PDB:2AG0, ECO:0000313|PDB:2AG1, FT ECO:0000313|PDB:2UZ1, ECO:0000313|PDB: FT 3IAF}. FT REGION 448 453 Thiaminepyrophosphate 2 binding. {ECO: FT 0000313|PDB:3IAF}. FT REGION 475 480 Thiaminepyrophosphate 1 binding. {ECO: FT 0000313|PDB:2AG0, ECO:0000313|PDB:2AG1, FT ECO:0000313|PDB:2UZ1, ECO:0000313|PDB: FT 3IAF}. FT REGION 475 480 Thiaminepyrophosphate 2 binding. {ECO: FT 0000313|PDB:3IAF}. FT ACT_SITE 29 29 Proton donor/acceptor. {ECO:0000313|PDB: FT 2AG0}. FT METAL 448 448 Calcium 1. {ECO:0000313|PDB:3IAE}. FT METAL 448 448 Calcium 2. {ECO:0000313|PDB:3D7K}. FT METAL 448 448 Magnesium. FT METAL 473 473 Calcium 1; via carbonyl oxygen. {ECO: FT 0000313|PDB:3IAE}. FT METAL 475 475 Calcium 1. {ECO:0000313|PDB:3IAE}. FT METAL 475 475 Calcium 2. {ECO:0000313|PDB:3D7K}. FT METAL 475 475 Magnesium. FT METAL 477 477 Calcium 2; via carbonyl oxygen. {ECO: FT 0000313|PDB:3D7K}. FT METAL 477 477 Magnesium; via carbonyl oxygen. FT BINDING 26 26 Thiaminepyrophosphate 4; via carbonyl FT oxygen. {ECO:0000313|PDB:2AG0}. FT BINDING 50 50 Thiaminepyrophosphate 1. {ECO: FT 0000313|PDB:3IAF}. FT BINDING 50 50 Thiaminepyrophosphate 2. {ECO: FT 0000313|PDB:3IAF}. FT BINDING 50 50 Thiaminepyrophosphate 3. {ECO: FT 0000313|PDB:2AG0, ECO:0000313|PDB:2AG1, FT ECO:0000313|PDB:2UZ1}. FT BINDING 50 50 Thiaminepyrophosphate 4. {ECO: FT 0000313|PDB:2AG0}. FT BINDING 50 50 Thiaminepyrophosphate 5. {ECO: FT 0000313|PDB:2AG0}. FT BINDING 76 76 Thiaminepyrophosphate 1. {ECO: FT 0000313|PDB:3IAF}. FT BINDING 76 76 Thiaminepyrophosphate 2. {ECO: FT 0000313|PDB:3IAF}. FT BINDING 76 76 Thiaminepyrophosphate 3. {ECO: FT 0000313|PDB:2AG0, ECO:0000313|PDB:2UZ1}. FT BINDING 113 113 Thiaminepyrophosphate 3. {ECO: FT 0000313|PDB:2AG1}. FT SITE 50 50 Important for catalytic activity. {ECO: FT 0000313|PDB:2AG0}. FT SITE 113 113 Transition state stabilizer. {ECO: FT 0000313|PDB:2AG0}. FT SITE 419 419 Important for catalytic activity. {ECO: FT 0000313|PDB:2AG0}. SQ SEQUENCE 563 AA; 58919 MW; 6511A404C501D126 CRC64; MAMITGGELV VRTLIKAGVE HLFGLHGAHI DTIFQACLDH DVPIIDTRHE AAAGHAAEGY ARAGAKLGVA LVTAGGGFTN AVTPIANAWL DRTPVLFLTG SGALRDDETN TLQAGIDQVA MAAPITKWAH RVMATEHIPR LVMQAIRAAL SAPRGPVLLD LPWDILMNQI DEDSVIIPDL VLSAHGARPD PADLDQALAL LRKAERPVIV LGSEASRTAR KTALSAFVAA TGVPVFADYE GLSMLSGLPD AMRGGLVQNL YSFAKADAAP DLVLMLGARF GLNTGHGSGQ LIPHSAQVIQ VDPDACELGR LQGIALGIVA DVGGTIEALA QATAQDAAWP DRGDWCAKVT DLAQERYASI AAKSSSEHAL HPFHASQVIA KHVDAGVTVV ADGALTYLWL SEVMSRVKPG GFLCHGYLGS MGVGFGTALG AQVADLEAGR RTILVTGDGS VGYSIGEFDT LVRKQLPLIV IIMNNQSWGA TLHFQQLAVG PNRVTGTRLE NGSYHGVAAA FGADGYHVDS VESFSAALAQ ALAHNRPACI NVAVALDPIP PEELILIGMD PFA //