ID Q9F4L3_PSEFL Unreviewed; 563 AA. AC Q9F4L3; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 91. DE SubName: Full=Benzaldehyde lyase {ECO:0000313|EMBL:AAG02282.1}; GN Name=bznB {ECO:0000313|EMBL:AAG02282.1}; OS Pseudomonas fluorescens. OC Bacteria; Pseudomonadota; 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 -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|ARBA:ARBA00001964}; 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 AlphaFoldDB; Q9F4L3; -. 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 GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt. DR CDD; cd02004; TPP_BZL_OCoD_HPCL; 1. DR CDD; cd07035; TPP_PYR_POX_like; 1. DR Gene3D; 3.40.50.970; -; 2. DR Gene3D; 3.40.50.1220; TPP-binding domain; 1. 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; IPR045229; TPP_enz. DR InterPro; IPR011766; TPP_enzyme_TPP-bd. DR PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 1. DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF00205; TPP_enzyme_M; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1}; KW Calcium {ECO:0007829|PDB:3D7K, ECO:0007829|PDB:3IAE}; KW Lyase {ECO:0000313|EMBL:AAG02282.1}; KW Metal-binding {ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1}; KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}. FT DOMAIN 5..121 FT /note="Thiamine pyrophosphate enzyme N-terminal TPP- FT binding" FT /evidence="ECO:0000259|Pfam:PF02776" FT DOMAIN 194..329 FT /note="Thiamine pyrophosphate enzyme central" FT /evidence="ECO:0000259|Pfam:PF00205" FT DOMAIN 397..542 FT /note="Thiamine pyrophosphate enzyme TPP-binding" FT /evidence="ECO:0000259|Pfam:PF02775" FT ACT_SITE 29 FT /note="EMO_00114 hydrogen bond donor,EMO_00114 hydrogen FT bond donor,EMO_00114 hydrogen bond donor,EMO_00114 hydrogen FT bond donor,EMO_00113 hydrogen bond acceptor,EMO_00114 FT hydrogen bond donor,EMO_00114 hydrogen bond donor,EMO_00068 FT proton donor,EMO_00068 proton donor,EMO_00066 proton FT acceptor,EMO_00066 proton acceptor" FT /evidence="ECO:0007829|PDB:2AG0" FT ACT_SITE 50 FT /note="EMO_00113 hydrogen bond acceptor,EMO_00114 hydrogen FT bond donor,EMO_00114 hydrogen bond donor,EMO_00114 hydrogen FT bond donor,EMO_00114 hydrogen bond donor,EMO_00114 hydrogen FT bond donor,EMO_00066 proton acceptor,EMO_00068 proton FT donor" FT /evidence="ECO:0007829|PDB:2AG0" FT BINDING 26 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4QPZ" FT BINDING 26 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:2AG0" FT BINDING 26 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4QPZ" FT BINDING 50 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 50 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:2AG0" FT BINDING 50 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ" FT BINDING 50 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:2AG0" FT BINDING 50 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ" FT BINDING 76 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2UZ1" FT BINDING 76 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ" FT BINDING 76 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ" FT BINDING 113 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4QPZ, ECO:0007829|PDB:4QQ8" FT BINDING 113 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2AG1" FT BINDING 113 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4QPZ, ECO:0007829|PDB:4QQ8" FT BINDING 393 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF" FT BINDING 393 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 394 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2UZ1" FT BINDING 395 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ" FT BINDING 395 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 396 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QQ8" FT BINDING 396 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 419 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF" FT BINDING 419 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 421 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ" FT BINDING 421 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2UZ1" FT BINDING 448 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3D7K" FT BINDING 448 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3IAE" FT BINDING 448 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 448 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 448 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ" FT BINDING 449 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 449 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ" FT BINDING 450 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ" FT BINDING 450 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 453 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG1, ECO:0007829|PDB:4QPZ" FT BINDING 453 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4QPZ" FT BINDING 473 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3IAE" FT BINDING 475 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3D7K" FT BINDING 475 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3IAE" FT BINDING 475 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 475 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ" FT BINDING 475 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 477 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3D7K" FT BINDING 477 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 477 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ" FT BINDING 477 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 478 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3IAF" FT BINDING 478 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF" FT BINDING 479 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF, ECO:0007829|PDB:4QPZ" FT BINDING 479 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT BINDING 480 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3IAF" FT BINDING 480 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2AG0, ECO:0007829|PDB:2AG1" FT SITE 113 FT /note="EMO_00113 hydrogen bond acceptor,EMO_00033 FT electrostatic stabiliser,EMO_00113 hydrogen bond FT acceptor,EMO_00033 electrostatic stabiliser,EMO_00113 FT hydrogen bond acceptor,EMO_00033 electrostatic FT stabiliser,EMO_00113 hydrogen bond acceptor,EMO_00033 FT electrostatic stabiliser,EMO_00113 hydrogen bond FT acceptor,EMO_00033 electrostatic stabiliser,EMO_00113 FT hydrogen bond acceptor,EMO_00033 electrostatic stabiliser" FT /evidence="ECO:0007829|PDB:2AG0" FT SITE 419 FT /note="EMO_00113 hydrogen bond acceptor,EMO_00033 FT electrostatic stabiliser,EMO_00113 hydrogen bond FT acceptor,EMO_00033 electrostatic stabiliser,EMO_00113 FT hydrogen bond acceptor,EMO_00033 electrostatic FT stabiliser,EMO_00113 hydrogen bond acceptor,EMO_00033 FT electrostatic stabiliser,EMO_00113 hydrogen bond FT acceptor,EMO_00033 electrostatic stabiliser,EMO_00113 FT hydrogen bond acceptor,EMO_00033 electrostatic stabiliser" 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 //