5DEI
BENZOYLFORMATE DECARBOXYLASE FROM PSEUDOMONAS PUTIDA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0003984 | molecular_function | acetolactate synthase activity |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0018924 | biological_process | mandelate metabolic process |
A | 0019439 | biological_process | obsolete aromatic compound catabolic process |
A | 0019596 | biological_process | mandelate catabolic process |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0050695 | molecular_function | benzoylformate decarboxylase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0003984 | molecular_function | acetolactate synthase activity |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0018924 | biological_process | mandelate metabolic process |
B | 0019439 | biological_process | obsolete aromatic compound catabolic process |
B | 0019596 | biological_process | mandelate catabolic process |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0050695 | molecular_function | benzoylformate decarboxylase activity |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0003984 | molecular_function | acetolactate synthase activity |
C | 0016831 | molecular_function | carboxy-lyase activity |
C | 0018924 | biological_process | mandelate metabolic process |
C | 0019439 | biological_process | obsolete aromatic compound catabolic process |
C | 0019596 | biological_process | mandelate catabolic process |
C | 0019752 | biological_process | carboxylic acid metabolic process |
C | 0030976 | molecular_function | thiamine pyrophosphate binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0050695 | molecular_function | benzoylformate decarboxylase activity |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0003984 | molecular_function | acetolactate synthase activity |
D | 0016831 | molecular_function | carboxy-lyase activity |
D | 0018924 | biological_process | mandelate metabolic process |
D | 0019439 | biological_process | obsolete aromatic compound catabolic process |
D | 0019596 | biological_process | mandelate catabolic process |
D | 0019752 | biological_process | carboxylic acid metabolic process |
D | 0030976 | molecular_function | thiamine pyrophosphate binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0050695 | molecular_function | benzoylformate decarboxylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue BCT A 601 |
Chain | Residue |
A | SER27 |
A | HIS71 |
A | LEU111 |
A | HOH1106 |
C | HIS282 |
C | TPP602 |
site_id | AC2 |
Number of Residues | 23 |
Details | binding site for residue TPP A 602 |
Chain | Residue |
A | LEU404 |
A | GLY428 |
A | ASP429 |
A | GLY430 |
A | SER431 |
A | TYR434 |
A | ASN456 |
A | THR458 |
A | TYR459 |
A | GLY460 |
A | ALA461 |
A | CA607 |
A | HOH757 |
C | ASN24 |
C | PRO25 |
C | GLY26 |
C | GLU48 |
C | HIS71 |
C | ASN78 |
C | BCT601 |
A | THR378 |
A | SER379 |
A | GLY402 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG A 603 |
Chain | Residue |
A | ASN118 |
A | LEU119 |
A | ARG121 |
C | ASN118 |
C | LEU119 |
C | ARG121 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue MG A 604 |
Chain | Residue |
A | LYS497 |
A | HOH1241 |
D | GLN494 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue MG A 605 |
Chain | Residue |
A | ARG185 |
A | HOH871 |
D | ASP188 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue CA A 606 |
Chain | Residue |
A | ASP188 |
D | ARG185 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue CA A 607 |
Chain | Residue |
A | ASP429 |
A | ASN456 |
A | THR458 |
A | TPP602 |
A | HOH752 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue BCT B 601 |
Chain | Residue |
B | SER27 |
B | HIS71 |
B | LEU111 |
B | HOH1107 |
D | HIS282 |
D | PHE465 |
D | TPP602 |
site_id | AC9 |
Number of Residues | 23 |
Details | binding site for residue TPP B 602 |
Chain | Residue |
B | THR378 |
B | SER379 |
B | GLY402 |
B | LEU404 |
B | GLY428 |
B | ASP429 |
B | GLY430 |
B | SER431 |
B | TYR434 |
B | ASN456 |
B | THR458 |
B | TYR459 |
B | GLY460 |
B | ALA461 |
B | CA607 |
B | HOH711 |
B | HOH765 |
D | ASN24 |
D | PRO25 |
D | GLU48 |
D | HIS71 |
D | ASN78 |
D | BCT601 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MG B 603 |
Chain | Residue |
B | ASN118 |
B | LEU119 |
B | ARG121 |
D | ASN118 |
D | LEU119 |
D | ARG121 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue MG B 604 |
Chain | Residue |
B | ARG185 |
B | HOH956 |
C | ASP188 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue MG B 605 |
Chain | Residue |
B | LYS497 |
B | HOH970 |
B | HOH1042 |
C | GLN494 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue MG B 606 |
Chain | Residue |
B | GLN494 |
C | LYS497 |
C | HOH1168 |
C | HOH1252 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue CA B 607 |
Chain | Residue |
B | HOH763 |
B | ASP429 |
B | ASN456 |
B | THR458 |
B | TPP602 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue CA B 608 |
Chain | Residue |
B | ASP188 |
C | ARG185 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue BCT C 601 |
Chain | Residue |
A | HIS282 |
A | LEU462 |
A | PHE465 |
A | TPP602 |
C | SER27 |
C | HIS71 |
C | LEU111 |
site_id | AD8 |
Number of Residues | 23 |
Details | binding site for residue TPP C 602 |
Chain | Residue |
A | ASN24 |
A | PRO25 |
A | GLY26 |
A | GLU48 |
A | HIS71 |
A | ASN78 |
A | BCT601 |
C | THR378 |
C | SER379 |
C | GLY402 |
C | LEU404 |
C | GLY428 |
C | ASP429 |
C | GLY430 |
C | SER431 |
C | TYR434 |
C | ASN456 |
C | THR458 |
C | TYR459 |
C | GLY460 |
C | ALA461 |
C | CA603 |
C | HOH761 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue CA C 603 |
Chain | Residue |
C | ASP429 |
C | ASN456 |
C | THR458 |
C | TPP602 |
C | HOH743 |
site_id | AE1 |
Number of Residues | 7 |
Details | binding site for residue BCT D 601 |
Chain | Residue |
B | HIS282 |
B | LEU462 |
B | TPP602 |
B | HOH1091 |
D | SER27 |
D | HIS71 |
D | LEU111 |
site_id | AE2 |
Number of Residues | 23 |
Details | binding site for residue TPP D 602 |
Chain | Residue |
B | ASN24 |
B | PRO25 |
B | GLY26 |
B | GLU48 |
B | HIS71 |
B | ASN78 |
B | BCT601 |
D | THR378 |
D | SER379 |
D | GLY402 |
D | LEU404 |
D | GLY428 |
D | ASP429 |
D | GLY430 |
D | SER431 |
D | TYR434 |
D | ASN456 |
D | THR458 |
D | TYR459 |
D | GLY460 |
D | ALA461 |
D | CA604 |
D | HOH779 |
site_id | AE3 |
Number of Residues | 2 |
Details | binding site for residue MG D 603 |
Chain | Residue |
A | GLN494 |
D | LYS497 |
site_id | AE4 |
Number of Residues | 5 |
Details | binding site for residue CA D 604 |
Chain | Residue |
D | ASP429 |
D | ASN456 |
D | THR458 |
D | TPP602 |
D | HOH749 |
Functional Information from PROSITE/UniProt
site_id | PS00187 |
Number of Residues | 20 |
Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGvqlaePerqvIaViGDGS |
Chain | Residue | Details |
A | ILE412-SER431 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | BINDING: |
Chain | Residue | Details |
B | ARG121 | |
B | ASP429 | |
B | ASN456 | |
B | THR458 | |
C | ASN118 | |
C | LEU119 | |
C | ARG121 | |
C | ASP429 | |
C | ASN456 | |
C | THR458 | |
D | ASN118 | |
D | LEU119 | |
D | ARG121 | |
D | ASP429 | |
D | ASN456 | |
D | THR458 | |
A | ASN118 | |
A | LEU119 | |
A | ARG121 | |
A | ASP429 | |
A | ASN456 | |
A | THR458 | |
B | ASN118 | |
B | LEU119 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 220 |
Chain | Residue | Details |
A | GLY26 | electrostatic stabiliser, hydrogen bond donor |
A | SER27 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | GLU29 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLU48 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | HIS71 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | HIS282 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLY402 | electrostatic stabiliser, hydrogen bond acceptor |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 220 |
Chain | Residue | Details |
B | GLY26 | electrostatic stabiliser, hydrogen bond donor |
B | SER27 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
B | GLU29 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | GLU48 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | HIS71 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | HIS282 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | GLY402 | electrostatic stabiliser, hydrogen bond acceptor |
site_id | MCSA3 |
Number of Residues | 7 |
Details | M-CSA 220 |
Chain | Residue | Details |
C | GLY26 | electrostatic stabiliser, hydrogen bond donor |
C | SER27 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
C | GLU29 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | GLU48 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | HIS71 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | HIS282 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | GLY402 | electrostatic stabiliser, hydrogen bond acceptor |
site_id | MCSA4 |
Number of Residues | 7 |
Details | M-CSA 220 |
Chain | Residue | Details |
D | GLY26 | electrostatic stabiliser, hydrogen bond donor |
D | SER27 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
D | GLU29 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | GLU48 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | HIS71 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
D | HIS282 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | GLY402 | electrostatic stabiliser, hydrogen bond acceptor |