ID MDLC_PSEPU Reviewed; 528 AA. AC P20906; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 13-SEP-2023, entry version 131. DE RecName: Full=Benzoylformate decarboxylase; DE Short=BFD; DE Short=BFDC; DE EC=4.1.1.7; GN Name=mdlC; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-19. RC STRAIN=ATCC 12633 / DSM 291 / JCM 13063 / CCUG 12690 / LMG 2257 / NBRC RC 14164 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90; RX PubMed=2271624; DOI=10.1021/bi00494a015; RA Tsou A.Y., Ransom S.C., Gerlt J.A., Buechter D.D., Babbitt P.C., RA Kenyon G.L.; RT "Mandelate pathway of Pseudomonas putida: sequence relationships involving RT mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate RT decarboxylase and expression of benzoylformate decarboxylase in Escherichia RT coli."; RL Biochemistry 29:9856-9862(1990). RN [2] RP CHARACTERIZATION, AND CRYSTALLIZATION. RC STRAIN=ATCC 12633 / DSM 291 / JCM 13063 / CCUG 12690 / LMG 2257 / NBRC RC 14164 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90; RX PubMed=7663351; DOI=10.1002/pro.5560040515; RA Hasson M.S., Muscate A., Henehan G.T.M., Guidinger P.F., Petsko G.A., RA Ringe D., Kenyon G.L.; RT "Purification and crystallization of benzoylformate decarboxylase."; RL Protein Sci. 4:955-959(1995). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SEQUENCE REVISION TO C-TERMINUS. RC STRAIN=ATCC 12633 / DSM 291 / JCM 13063 / CCUG 12690 / LMG 2257 / NBRC RC 14164 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90; RX PubMed=9665697; DOI=10.1021/bi973047e; RA Hasson M.S., Muscate A., McLeish M.J., Polovnikova L.S., Gerlt J.A., RA Kenyon G.L., Petsko G.A., Ringe D.; RT "The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: RT diversity of catalytic residues in thiamin diphosphate-dependent enzymes."; RL Biochemistry 37:9918-9930(1998). CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + phenylglyoxylate = benzaldehyde + CO2; CC Xref=Rhea:RHEA:23368, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:17169, ChEBI:CHEBI:36656; EC=4.1.1.7; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 1 Ca(2+) ion per subunit.; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Note=Binds 1 thiamine pyrophosphate per subunit.; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per dimer.; CC -!- PATHWAY: Aromatic compound metabolism; (R)-mandelate degradation; CC benzoate from (R)-mandelate: step 3/4. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}. 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; AY143338; AAC15502.1; -; Genomic_DNA. DR PIR; C44767; C44767. DR RefSeq; WP_016501746.1; NZ_UGUX01000003.1. DR PDB; 1BFD; X-ray; 1.60 A; A=1-528. DR PDB; 1MCZ; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-528. DR PDB; 1PI3; X-ray; 1.20 A; A=1-528. DR PDB; 1PO7; X-ray; 1.20 A; A=1-528. DR PDB; 1Q6Z; X-ray; 1.00 A; A=1-528. DR PDB; 1YNO; X-ray; 1.22 A; A=2-528. DR PDB; 2FN3; X-ray; 1.00 A; A=1-528. DR PDB; 2FWN; X-ray; 1.40 A; A=1-528. DR PDB; 2V3W; X-ray; 2.20 A; A/B/C/D=1-528. DR PDB; 3F6B; X-ray; 1.34 A; X=2-526. DR PDB; 3F6E; X-ray; 1.34 A; X=2-526. DR PDB; 3FSJ; X-ray; 1.37 A; X=1-528. DR PDB; 3FZN; X-ray; 1.62 A; A/B/C/D=1-528. DR PDB; 4GG1; X-ray; 1.07 A; A=1-528. DR PDB; 4GM0; X-ray; 1.07 A; A=1-528. DR PDB; 4GM1; X-ray; 1.26 A; A=1-528. DR PDB; 4GM4; X-ray; 1.28 A; A=1-528. DR PDB; 4GP9; X-ray; 1.07 A; A=1-528. DR PDB; 4GPE; X-ray; 1.39 A; A=1-528. DR PDB; 4JD5; X-ray; 1.33 A; A=1-528. DR PDB; 4JU8; X-ray; 1.25 A; A=1-528. DR PDB; 4JU9; X-ray; 1.12 A; A=1-528. DR PDB; 4JUA; X-ray; 1.15 A; A=1-528. DR PDB; 4JUB; X-ray; 1.90 A; A/B/C/D=1-528. DR PDB; 4JUC; X-ray; 2.30 A; A/B/C/D=1-528. DR PDB; 4JUD; X-ray; 1.65 A; X=1-528. DR PDB; 4JUF; X-ray; 2.15 A; A/B/C/D=2-528. DR PDB; 4K9K; X-ray; 1.30 A; A=2-525. DR PDB; 4K9L; X-ray; 1.65 A; A=2-526. DR PDB; 4K9M; X-ray; 1.15 A; A=2-525. DR PDB; 4K9N; X-ray; 1.70 A; A/B/C/D=2-525. DR PDB; 4K9O; X-ray; 1.89 A; A/B/C/D=2-528. DR PDB; 4K9P; X-ray; 2.24 A; A/B/C/D=2-528. DR PDB; 4MPJ; X-ray; 1.50 A; A=1-528. DR PDB; 4MPP; X-ray; 1.50 A; A=1-528. DR PDB; 4MPR; X-ray; 1.40 A; A=1-528. DR PDB; 4MQ5; X-ray; 1.50 A; A=1-528. DR PDB; 4MZX; X-ray; 1.56 A; A=1-528. DR PDB; 4QEL; X-ray; 1.43 A; A=1-528. DR PDB; 5DEI; X-ray; 1.30 A; A/B/C/D=2-525. DR PDB; 5DGD; X-ray; 1.13 A; A=2-525. DR PDB; 5DGT; X-ray; 1.08 A; A=2-525. DR PDB; 6M2Y; X-ray; 2.10 A; A=1-528. DR PDB; 6M2Z; X-ray; 2.35 A; A=1-528. DR PDBsum; 1BFD; -. DR PDBsum; 1MCZ; -. DR PDBsum; 1PI3; -. DR PDBsum; 1PO7; -. DR PDBsum; 1Q6Z; -. DR PDBsum; 1YNO; -. DR PDBsum; 2FN3; -. DR PDBsum; 2FWN; -. DR PDBsum; 2V3W; -. DR PDBsum; 3F6B; -. DR PDBsum; 3F6E; -. DR PDBsum; 3FSJ; -. DR PDBsum; 3FZN; -. DR PDBsum; 4GG1; -. DR PDBsum; 4GM0; -. DR PDBsum; 4GM1; -. DR PDBsum; 4GM4; -. DR PDBsum; 4GP9; -. DR PDBsum; 4GPE; -. DR PDBsum; 4JD5; -. DR PDBsum; 4JU8; -. DR PDBsum; 4JU9; -. DR PDBsum; 4JUA; -. DR PDBsum; 4JUB; -. DR PDBsum; 4JUC; -. DR PDBsum; 4JUD; -. DR PDBsum; 4JUF; -. DR PDBsum; 4K9K; -. DR PDBsum; 4K9L; -. DR PDBsum; 4K9M; -. DR PDBsum; 4K9N; -. DR PDBsum; 4K9O; -. DR PDBsum; 4K9P; -. DR PDBsum; 4MPJ; -. DR PDBsum; 4MPP; -. DR PDBsum; 4MPR; -. DR PDBsum; 4MQ5; -. DR PDBsum; 4MZX; -. DR PDBsum; 4QEL; -. DR PDBsum; 5DEI; -. DR PDBsum; 5DGD; -. DR PDBsum; 5DGT; -. DR PDBsum; 6M2Y; -. DR PDBsum; 6M2Z; -. DR AlphaFoldDB; P20906; -. DR SMR; P20906; -. DR DrugBank; DB02280; (R)-Mandelic acid. DR DrugBank; DB01987; Cocarboxylase. DR GeneID; 45526286; -. DR BioCyc; MetaCyc:MONOMER-2461; -. DR BRENDA; 4.1.1.7; 5092. DR SABIO-RK; P20906; -. DR UniPathway; UPA00873; UER00854. DR EvolutionaryTrace; P20906; -. DR GO; GO:0050695; F:benzoylformate decarboxylase 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:0019596; P:mandelate catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd02002; TPP_BFDC; 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; IPR000399; TPP-bd_CS. DR InterPro; IPR045229; TPP_enz. DR InterPro; IPR011766; TPP_enzyme_TPP-bd. DR PANTHER; PTHR18968:SF133; BENZOYLFORMATE DECARBOXYLASE; 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. DR PROSITE; PS00187; TPP_ENZYMES; 1. PE 1: Evidence at protein level; KW 3D-structure; Aromatic hydrocarbons catabolism; Calcium; Decarboxylase; KW Direct protein sequencing; Lyase; Magnesium; Mandelate pathway; KW Metal-binding; Thiamine pyrophosphate. FT CHAIN 1..528 FT /note="Benzoylformate decarboxylase" FT /id="PRO_0000090820" FT REGION 377..460 FT /note="Thiamine pyrophosphate binding" FT BINDING 117 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 118 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 120 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 428 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 455 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 457 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT HELIX 4..14 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 19..22 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 29..32 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 47..61 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 65..70 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 71..77 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 79..87 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 92..98 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 101..104 FT /evidence="ECO:0007829|PDB:1Q6Z" FT TURN 105..107 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:1Q6Z" FT TURN 118..121 FT /evidence="ECO:0007829|PDB:2FN3" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:4K9K" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 135..147 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 160..162 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 169..174 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:5DEI" FT HELIX 187..199 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 209..213 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 217..227 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 249..252 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 257..264 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 268..275 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 294..300 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 302..307 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 309..316 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 318..328 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 350..353 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 355..365 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 371..375 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 377..379 FT /evidence="ECO:0007829|PDB:4GP9" FT HELIX 380..386 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 391..393 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 395..397 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 403..405 FT /evidence="ECO:0007829|PDB:4GM4" FT HELIX 406..416 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 422..427 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 428..431 FT /evidence="ECO:0007829|PDB:1Q6Z" FT TURN 432..434 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 435..437 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 438..444 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 449..454 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 459..468 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 483..490 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 493..499 FT /evidence="ECO:0007829|PDB:1Q6Z" FT HELIX 500..511 FT /evidence="ECO:0007829|PDB:1Q6Z" FT STRAND 517..523 FT /evidence="ECO:0007829|PDB:1Q6Z" SQ SEQUENCE 528 AA; 56355 MW; DDB7BC03AD866CC1 CRC64; MASVHGTTYE LLRRQGIDTV FGNPGSNELP FLKDFPEDFR YILALQEACV VGIADGYAQA SRKPAFINLH SAAGTGNAMG ALSNAWNSHS PLIVTAGQQT RAMIGVEALL TNVDAANLPR PLVKWSYEPA SAAEVPHAMS RAIHMASMAP QGPVYLSVPY DDWDKDADPQ SHHLFDRHVS SSVRLNDQDL DILVKALNSA SNPAIVLGPD VDAANANADC VMLAERLKAP VWVAPSAPRC PFPTRHPCFR GLMPAGIAAI SQLLEGHDVV LVIGAPVFRY HQYDPGQYLK PGTRLISVTC DPLEAARAPM GDAIVADIGA MASALANLVE ESSRQLPTAA PEPAKVDQDA GRLHPETVFD TLNDMAPENA IYLNESTSTT AQMWQRLNMR NPGSYYFCAA GGLGFALPAA IGVQLAEPER QVIAVIGDGS ANYSISALWT AAQYNIPTIF VIMNNGTYGA LRWFAGVLEA ENVPGLDVPG IDFRALAKGY GVQALKADNL EQLKGSLQEA LSAKGPVLIE VSTVSPVK //