5EXD
Crystal structure of oxalate oxidoreductase from Moorella thermoacetica bound with carboxy-di-oxido-methyl-TPP (COOM-TPP) intermediate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0006979 | biological_process | response to oxidative stress |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
A | 0033611 | biological_process | oxalate catabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
B | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
B | 0033611 | biological_process | oxalate catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
C | 0030976 | molecular_function | thiamine pyrophosphate binding |
C | 0033611 | biological_process | oxalate catabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0006979 | biological_process | response to oxidative stress |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
D | 0033611 | biological_process | oxalate catabolic process |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
E | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
E | 0033611 | biological_process | oxalate catabolic process |
E | 0046872 | molecular_function | metal ion binding |
E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
F | 0003824 | molecular_function | catalytic activity |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
F | 0030976 | molecular_function | thiamine pyrophosphate binding |
F | 0033611 | biological_process | oxalate catabolic process |
F | 0046872 | molecular_function | metal ion binding |
F | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
G | 0003824 | molecular_function | catalytic activity |
G | 0006979 | biological_process | response to oxidative stress |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
G | 0033611 | biological_process | oxalate catabolic process |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
H | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
H | 0033611 | biological_process | oxalate catabolic process |
H | 0046872 | molecular_function | metal ion binding |
H | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
I | 0003824 | molecular_function | catalytic activity |
I | 0016491 | molecular_function | oxidoreductase activity |
I | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
I | 0030976 | molecular_function | thiamine pyrophosphate binding |
I | 0033611 | biological_process | oxalate catabolic process |
I | 0046872 | molecular_function | metal ion binding |
I | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
J | 0003824 | molecular_function | catalytic activity |
J | 0006979 | biological_process | response to oxidative stress |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
J | 0033611 | biological_process | oxalate catabolic process |
K | 0016491 | molecular_function | oxidoreductase activity |
K | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
K | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
K | 0033611 | biological_process | oxalate catabolic process |
K | 0046872 | molecular_function | metal ion binding |
K | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
L | 0003824 | molecular_function | catalytic activity |
L | 0016491 | molecular_function | oxidoreductase activity |
L | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
L | 0030976 | molecular_function | thiamine pyrophosphate binding |
L | 0033611 | biological_process | oxalate catabolic process |
L | 0046872 | molecular_function | metal ion binding |
L | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue SF4 B 401 |
Chain | Residue |
B | CYS271 |
B | CYS290 |
B | LYS291 |
B | GLY292 |
B | CYS293 |
B | GLY294 |
B | CYS296 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue SF4 B 402 |
Chain | Residue |
B | GLU263 |
B | CYS264 |
B | TYR265 |
B | CYS267 |
B | CYS300 |
B | SER302 |
B | CYS261 |
B | THR262 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue SF4 C 401 |
Chain | Residue |
C | CYS24 |
C | CYS27 |
C | PRO29 |
C | CYS52 |
C | ASN138 |
C | ALA142 |
C | CYS225 |
C | PRO226 |
C | LYS227 |
site_id | AC4 |
Number of Residues | 23 |
Details | binding site for residue TPP C 402 |
Chain | Residue |
A | TYR28 |
A | PRO29 |
A | ILE30 |
A | GLU59 |
A | VAL83 |
C | THR50 |
C | GLY51 |
C | CYS52 |
C | ILE74 |
C | GLY109 |
C | ASP110 |
C | GLY111 |
C | GLY112 |
C | TYR136 |
C | ASN138 |
C | SER140 |
C | TYR141 |
C | ALA142 |
C | ASN143 |
C | THR144 |
C | MG403 |
C | HOH501 |
D | GLU90 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue MG C 403 |
Chain | Residue |
C | ASP110 |
C | ASN138 |
C | SER140 |
C | TPP402 |
C | HOH501 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue SF4 E 401 |
Chain | Residue |
E | CYS271 |
E | PHE285 |
E | CYS290 |
E | GLY292 |
E | CYS293 |
E | GLY294 |
E | CYS296 |
site_id | AC7 |
Number of Residues | 10 |
Details | binding site for residue SF4 E 402 |
Chain | Residue |
E | CYS261 |
E | THR262 |
E | GLU263 |
E | CYS264 |
E | TYR265 |
E | CYS267 |
E | PRO283 |
E | CYS300 |
E | PRO301 |
E | SER302 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue SF4 F 401 |
Chain | Residue |
E | ARG58 |
F | CYS24 |
F | CYS27 |
F | PRO29 |
F | CYS52 |
F | ASN138 |
F | CYS225 |
F | PRO226 |
site_id | AC9 |
Number of Residues | 24 |
Details | binding site for residue O2T F 402 |
Chain | Residue |
F | MG403 |
F | HOH501 |
A | GLU90 |
D | TYR28 |
D | PRO29 |
D | ILE30 |
D | ARG31 |
D | GLU59 |
D | ARG109 |
D | ASP116 |
F | THR50 |
F | GLY51 |
F | CYS52 |
F | ILE74 |
F | ASP110 |
F | GLY111 |
F | GLY112 |
F | TYR136 |
F | ASN138 |
F | SER140 |
F | TYR141 |
F | ALA142 |
F | ASN143 |
F | THR144 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue MG F 403 |
Chain | Residue |
F | ASP110 |
F | ASN138 |
F | SER140 |
F | O2T402 |
F | HOH501 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue SF4 H 401 |
Chain | Residue |
H | CYS271 |
H | CYS290 |
H | LYS291 |
H | GLY292 |
H | CYS293 |
H | GLY294 |
H | CYS296 |
site_id | AD3 |
Number of Residues | 11 |
Details | binding site for residue SF4 H 402 |
Chain | Residue |
H | CYS261 |
H | THR262 |
H | GLU263 |
H | CYS264 |
H | TYR265 |
H | CYS267 |
H | PRO283 |
H | CYS300 |
H | PRO301 |
H | SER302 |
H | LEU305 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue SF4 I 401 |
Chain | Residue |
H | ARG58 |
I | CYS24 |
I | CYS27 |
I | PRO29 |
I | CYS52 |
I | ASN138 |
I | CYS225 |
I | PRO226 |
I | LYS227 |
site_id | AD5 |
Number of Residues | 23 |
Details | binding site for residue TPP I 402 |
Chain | Residue |
G | TYR28 |
G | PRO29 |
G | ILE30 |
G | GLU59 |
G | VAL83 |
I | THR50 |
I | GLY51 |
I | CYS52 |
I | ILE74 |
I | GLY109 |
I | ASP110 |
I | GLY111 |
I | GLY112 |
I | TYR136 |
I | ASN138 |
I | SER140 |
I | TYR141 |
I | ALA142 |
I | ASN143 |
I | THR144 |
I | MG403 |
I | HOH504 |
J | GLU90 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue MG I 403 |
Chain | Residue |
I | ASP110 |
I | ASN138 |
I | SER140 |
I | TPP402 |
I | HOH504 |
site_id | AD7 |
Number of Residues | 9 |
Details | binding site for residue SF4 K 401 |
Chain | Residue |
K | CYS271 |
K | ASP273 |
K | PHE285 |
K | CYS290 |
K | LYS291 |
K | GLY292 |
K | CYS293 |
K | GLY294 |
K | CYS296 |
site_id | AD8 |
Number of Residues | 11 |
Details | binding site for residue SF4 K 402 |
Chain | Residue |
K | CYS261 |
K | THR262 |
K | GLU263 |
K | CYS264 |
K | TYR265 |
K | CYS267 |
K | PRO283 |
K | CYS300 |
K | PRO301 |
K | SER302 |
K | LEU305 |
site_id | AD9 |
Number of Residues | 9 |
Details | binding site for residue SF4 L 401 |
Chain | Residue |
K | ARG58 |
L | CYS24 |
L | CYS27 |
L | PRO29 |
L | CYS52 |
L | ASN138 |
L | CYS225 |
L | PRO226 |
L | LYS227 |
site_id | AE1 |
Number of Residues | 22 |
Details | binding site for residue TPP L 402 |
Chain | Residue |
G | GLU90 |
J | PRO29 |
J | ILE30 |
J | GLU59 |
J | VAL83 |
L | THR50 |
L | GLY51 |
L | CYS52 |
L | ILE74 |
L | GLY109 |
L | ASP110 |
L | GLY111 |
L | GLY112 |
L | TYR136 |
L | ASN138 |
L | SER140 |
L | TYR141 |
L | ALA142 |
L | ASN143 |
L | THR144 |
L | MG403 |
L | HOH501 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue MG L 403 |
Chain | Residue |
L | ASP110 |
L | ASN138 |
L | SER140 |
L | TPP402 |
L | HOH501 |
Functional Information from PROSITE/UniProt
site_id | PS00198 |
Number of Residues | 12 |
Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CtECYtCWiYCP |
Chain | Residue | Details |
B | CYS261-PRO272 | |
B | CYS290-PRO301 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P94692 |
Chain | Residue | Details |
C | CYS24 | |
I | CYS27 | |
I | CYS52 | |
I | CYS225 | |
L | CYS24 | |
L | CYS27 | |
L | CYS52 | |
L | CYS225 | |
H | CYS261 | |
H | CYS264 | |
H | CYS267 | |
C | CYS27 | |
H | CYS271 | |
H | CYS290 | |
H | CYS293 | |
H | CYS296 | |
H | CYS300 | |
K | CYS261 | |
K | CYS264 | |
K | CYS267 | |
K | CYS271 | |
K | CYS290 | |
C | CYS52 | |
K | CYS293 | |
K | CYS296 | |
K | CYS300 | |
C | CYS225 | |
F | CYS24 | |
F | CYS27 | |
F | CYS52 | |
F | CYS225 | |
I | CYS24 |