ID   BZNB_PSEFL              Reviewed;         563 AA.
AC   P51853;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Benzaldehyde lyase;
DE            EC=4.1.2.38;
DE   AltName: Full=Benzoin aldolase;
DE            Short=BL;
DE            Short=BZL;
GN   Name=bznB;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Biovar I;
RX   PubMed=8026749; DOI=10.1016/0378-1119(94)90218-6;
RA   Hinrichsen P., Gomez I., Vicuna R.;
RT   "Cloning and sequencing of the gene encoding benzaldehyde lyase from
RT   Pseudomonas fluorescens biovar I.";
RL   Gene 144:137-138(1994).
CC   -!- FUNCTION: Cleavage of benzoin-anisoin acyloin linkage.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=benzoin = 2 benzaldehyde; Xref=Rhea:RHEA:21460,
CC         ChEBI:CHEBI:17169, ChEBI:CHEBI:17682; EC=4.1.2.38;
CC   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC       Note=Binds 1 metal ion per subunit.;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC       Note=Binds 1 thiamine pyrophosphate per subunit.;
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; U04048; AAA50176.1; -; Genomic_DNA.
DR   PDB; 2UZ1; X-ray; 1.65 A; B/C=1-563.
DR   PDB; 3D7K; X-ray; 2.49 A; A/B=1-562.
DR   PDBsum; 2UZ1; -.
DR   PDBsum; 3D7K; -.
DR   AlphaFoldDB; P51853; -.
DR   SMR; P51853; -.
DR   BRENDA; 4.1.2.38; 5121.
DR   SABIO-RK; P51853; -.
DR   EvolutionaryTrace; P51853; -.
DR   GO; GO:0047695; F:benzoin aldolase activity; IEA:UniProtKB-EC.
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   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-bd_C.
DR   PANTHER; PTHR18968; PTHR18968; 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; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Lyase; Thiamine pyrophosphate.
FT   CHAIN           1..563
FT                   /note="Benzaldehyde lyase"
FT                   /id="PRO_0000090827"
SQ   SEQUENCE   563 AA;  58957 MW;  36940C0B33265DBF CRC64;
     MAMITGGELV VRTLIKAGVE HLFGLHGAHI DTIFQACLDH DVPIIDTRHE AAAGHAAEGY
     ARAGAKLGVA GHGGRGIYQC GHAHCQRLAG SQGRCIPHPG 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