ID Q9F4L3_PSEFL Unreviewed; 563 AA. AC Q9F4L3; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 07-APR-2021, entry version 83. 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 Gourlay C.W., Hofer J., Ellis N.; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1} RP X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND RP THIAMINE PYROPHOSPHATE, 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:0007829|PDB:2UZ1} RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH THIAMINE RP PYROPHOSPHATE. RX PubMed=17620706; DOI=10.1107/S1744309107028576; 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 1.65 RT A resolution."; RL Acta Crystallogr. F Struct. Biol. Commun. 63:546-548(2007). RN [4] {ECO:0007829|PDB:3D7K} RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-562 IN COMPLEX WITH CALCIUM. RX PubMed=18570438; DOI=10.1021/bi8004413; RA Brandt G.S., Nemeria N., Chakraborty S., McLeish M.J., Yep A., Kenyon G.L., RA Petsko G.A., Jordan F., Ringe D.; RT "Probing the active center of benzaldehyde lyase with substitutions and the RT pseudosubstrate analogue benzoylphosphonic acid methyl ester."; RL Biochemistry 47:7734-7743(2008). RN [5] {ECO:0007829|PDB:3IAE, ECO:0007829|PDB:3IAF} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-562 IN COMPLEX WITH CALCIUM; RP MAGNESIUM AND THIAMINE PYROPHOSPHATE. 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 mutation RT can confer both new reactivity and susceptibility to mechanism-based RT inhibition."; RL J. Am. Chem. Soc. 132:438-439(2010). RN [6] {ECO:0007829|PDB:4QPZ, ECO:0007829|PDB:4QQ8} RP X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND RP THIAMINE PYROPHOSPHATE. RX PubMed=25775555; DOI=10.1073/pnas.1500545112; RA Siegel J.B., Smith A.L., Poust S., Wargacki A.J., Bar-Even A., Louw C., RA Shen B.W., Eiben C.B., Tran H.M., Noor E., Gallaher J.L., Bale J., RA Yoshikuni Y., Gelb M.H., Keasling J.D., Stoddard B.L., Lidstrom M.E., RA Baker D.; RT "Computational protein design enables a novel one-carbon assimilation RT pathway."; RL Proc. Natl. Acad. Sci. U.S.A. 112:3704-3709(2015). CC -!- SIMILARITY: Belongs to the TPP enzyme family. CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}. 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 PDB; 4QPZ; X-ray; 3.00 A; A/B/C/D/E/F/G/H=2-563. DR PDB; 4QQ8; X-ray; 2.88 A; A/B/C/D=1-563. DR PDBsum; 2AG0; -. DR PDBsum; 2AG1; -. DR PDBsum; 2UZ1; -. DR PDBsum; 3D7K; -. DR PDBsum; 3IAE; -. DR PDBsum; 3IAF; -. DR PDBsum; 4QPZ; -. DR PDBsum; 4QQ8; -. DR SMR; Q9F4L3; -. 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 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:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1, KW ECO:0007829|PDB:2UZ1, ECO:0007829|PDB:3D7K}; KW Calcium {ECO:0007829|PDB:3D7K, ECO:0007829|PDB:3IAE}; KW Lyase {ECO:0000313|EMBL:AAG02282.1}; KW Magnesium {ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1, KW ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ}; KW Metal-binding {ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1, KW ECO:0007829|PDB:3D7K, ECO:0007829|PDB:3IAE}; KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132, KW ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1, ECO:0007829|PDB:2UZ1}. FT DOMAIN 5..173 FT /note="TPP_enzyme_N" FT /evidence="ECO:0000259|Pfam:PF02776" FT DOMAIN 194..329 FT /note="TPP_enzyme_M" FT /evidence="ECO:0000259|Pfam:PF00205" FT DOMAIN 397..542 FT /note="TPP_enzyme_C" FT /evidence="ECO:0000259|Pfam:PF02775" FT REGION 393..396 FT /note="Thiamine pyrophosphate 1 binding" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1, FT ECO:0007829|PDB:2UZ1" FT REGION 393..396 FT /note="Thiamine pyrophosphate 2 binding" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ, FT ECO:0007829|PDB:4QQ8" FT REGION 419..421 FT /note="Thiamine pyrophosphate 1 binding" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1, FT ECO:0007829|PDB:2UZ1" FT REGION 419..421 FT /note="Thiamine pyrophosphate 2 binding" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ, FT ECO:0007829|PDB:4QQ8" FT REGION 448..453 FT /note="Thiamine pyrophosphate 1 binding" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1, FT ECO:0007829|PDB:2UZ1" FT REGION 448..453 FT /note="Thiamine pyrophosphate 2 binding" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ, FT ECO:0007829|PDB:4QQ8" FT REGION 475..480 FT /note="Thiamine pyrophosphate 1 binding" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1, FT ECO:0007829|PDB:2UZ1" FT REGION 475..480 FT /note="Thiamine pyrophosphate 2 binding" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ, FT ECO:0007829|PDB:4QQ8" FT ACT_SITE 29 FT /note="Proton donor/acceptor" FT /evidence="ECO:0007829|PDB:2AG0" FT METAL 448 FT /note="Calcium 1" FT /evidence="ECO:0007829|PDB:3IAE" FT METAL 448 FT /note="Calcium 2" FT /evidence="ECO:0007829|PDB:3D7K" FT METAL 448 FT /note="Magnesium" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1, FT ECO:0007829|PDB:4QPZ" FT METAL 473 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:3IAE" FT METAL 475 FT /note="Calcium 1" FT /evidence="ECO:0007829|PDB:3IAE" FT METAL 475 FT /note="Calcium 2" FT /evidence="ECO:0007829|PDB:3D7K" FT METAL 475 FT /note="Magnesium" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1, FT ECO:0007829|PDB:4QPZ" FT METAL 477 FT /note="Calcium 2; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:3D7K" FT METAL 477 FT /note="Magnesium; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1, FT ECO:0007829|PDB:4QPZ" FT BINDING 26 FT /note="Thiamine pyrophosphate 1; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:4QPZ" FT BINDING 26 FT /note="Thiamine pyrophosphate 2; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:4QPZ" FT BINDING 26 FT /note="Thiamine pyrophosphate 4; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:2AG0" FT BINDING 50 FT /note="Thiamine pyrophosphate 1" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ, FT ECO:0007829|PDB:4QQ8" FT BINDING 50 FT /note="Thiamine pyrophosphate 2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ, FT ECO:0007829|PDB:4QQ8" FT BINDING 50 FT /note="Thiamine pyrophosphate 3" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1, FT ECO:0007829|PDB:2UZ1" FT BINDING 50 FT /note="Thiamine pyrophosphate 4" FT /evidence="ECO:0007829|PDB:2AG0" FT BINDING 50 FT /note="Thiamine pyrophosphate 5" FT /evidence="ECO:0007829|PDB:2AG0" FT BINDING 76 FT /note="Thiamine pyrophosphate 1" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ, FT ECO:0007829|PDB:4QQ8" FT BINDING 76 FT /note="Thiamine pyrophosphate 2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ, FT ECO:0007829|PDB:4QQ8" FT BINDING 76 FT /note="Thiamine pyrophosphate 3" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2UZ1" FT BINDING 113 FT /note="Thiamine pyrophosphate 1" FT /evidence="ECO:0007829|PDB:4QPZ, ECO:0007829|PDB:4QQ8" FT BINDING 113 FT /note="Thiamine pyrophosphate 2" FT /evidence="ECO:0007829|PDB:4QPZ, ECO:0007829|PDB:4QQ8" FT BINDING 113 FT /note="Thiamine pyrophosphate 3" FT /evidence="ECO:0007829|PDB:2AG1" FT SITE 50 FT /note="Important for catalytic activity" FT /evidence="ECO:0007829|PDB:2AG0" FT SITE 113 FT /note="Transition state stabilizer" FT /evidence="ECO:0007829|PDB:2AG0" FT SITE 419 FT /note="Important for catalytic activity" FT /evidence="ECO:0007829|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 //