Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

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	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	0016903	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors
A	0019752	biological_process	carboxylic acid metabolic process
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	0051536	molecular_function	iron-sulfur cluster 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	0051536	molecular_function	iron-sulfur cluster binding
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
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	0016903	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors
D	0019752	biological_process	carboxylic acid metabolic process
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	0051536	molecular_function	iron-sulfur cluster 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	0051536	molecular_function	iron-sulfur cluster binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
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	0016903	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors
G	0019752	biological_process	carboxylic acid metabolic process
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	0051536	molecular_function	iron-sulfur cluster 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	0051536	molecular_function	iron-sulfur cluster binding
I	0051539	molecular_function	4 iron, 4 sulfur cluster binding
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	0016903	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors
J	0019752	biological_process	carboxylic acid metabolic process
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	0051536	molecular_function	iron-sulfur cluster 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	0051536	molecular_function	iron-sulfur cluster 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	112
Details	Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	116
Details	Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P94692","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)