Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6YBP

Propionyl-CoA carboxylase of Methylorubrum extorquens with bound CoA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003989	molecular_function	acetyl-CoA carboxylase activity
A	0004658	molecular_function	propionyl-CoA carboxylase activity
A	0009317	cellular_component	acetyl-CoA carboxylase complex
A	0015977	biological_process	carbon fixation
A	0016874	molecular_function	ligase activity
B	0003989	molecular_function	acetyl-CoA carboxylase activity
B	0004658	molecular_function	propionyl-CoA carboxylase activity
B	0009317	cellular_component	acetyl-CoA carboxylase complex
B	0015977	biological_process	carbon fixation
B	0016874	molecular_function	ligase activity
C	0003989	molecular_function	acetyl-CoA carboxylase activity
C	0004658	molecular_function	propionyl-CoA carboxylase activity
C	0009317	cellular_component	acetyl-CoA carboxylase complex
C	0015977	biological_process	carbon fixation
C	0016874	molecular_function	ligase activity
D	0003989	molecular_function	acetyl-CoA carboxylase activity
D	0004658	molecular_function	propionyl-CoA carboxylase activity
D	0009317	cellular_component	acetyl-CoA carboxylase complex
D	0015977	biological_process	carbon fixation
D	0016874	molecular_function	ligase activity
E	0003989	molecular_function	acetyl-CoA carboxylase activity
E	0004658	molecular_function	propionyl-CoA carboxylase activity
E	0009317	cellular_component	acetyl-CoA carboxylase complex
E	0015977	biological_process	carbon fixation
E	0016874	molecular_function	ligase activity
F	0003989	molecular_function	acetyl-CoA carboxylase activity
F	0004658	molecular_function	propionyl-CoA carboxylase activity
F	0009317	cellular_component	acetyl-CoA carboxylase complex
F	0015977	biological_process	carbon fixation
F	0016874	molecular_function	ligase activity
G	0000166	molecular_function	nucleotide binding
G	0004658	molecular_function	propionyl-CoA carboxylase activity
G	0005524	molecular_function	ATP binding
G	0006629	biological_process	lipid metabolic process
G	0016042	biological_process	lipid catabolic process
G	0016874	molecular_function	ligase activity
G	0046872	molecular_function	metal ion binding
H	0000166	molecular_function	nucleotide binding
H	0004658	molecular_function	propionyl-CoA carboxylase activity
H	0005524	molecular_function	ATP binding
H	0006629	biological_process	lipid metabolic process
H	0016042	biological_process	lipid catabolic process
H	0016874	molecular_function	ligase activity
H	0046872	molecular_function	metal ion binding
I	0000166	molecular_function	nucleotide binding
I	0004658	molecular_function	propionyl-CoA carboxylase activity
I	0005524	molecular_function	ATP binding
I	0006629	biological_process	lipid metabolic process
I	0016042	biological_process	lipid catabolic process
I	0016874	molecular_function	ligase activity
I	0046872	molecular_function	metal ion binding
J	0000166	molecular_function	nucleotide binding
J	0004658	molecular_function	propionyl-CoA carboxylase activity
J	0005524	molecular_function	ATP binding
J	0006629	biological_process	lipid metabolic process
J	0016042	biological_process	lipid catabolic process
J	0016874	molecular_function	ligase activity
J	0046872	molecular_function	metal ion binding
K	0000166	molecular_function	nucleotide binding
K	0004658	molecular_function	propionyl-CoA carboxylase activity
K	0005524	molecular_function	ATP binding
K	0006629	biological_process	lipid metabolic process
K	0016042	biological_process	lipid catabolic process
K	0016874	molecular_function	ligase activity
K	0046872	molecular_function	metal ion binding
L	0000166	molecular_function	nucleotide binding
L	0004658	molecular_function	propionyl-CoA carboxylase activity
L	0005524	molecular_function	ATP binding
L	0006629	biological_process	lipid metabolic process
L	0016042	biological_process	lipid catabolic process
L	0016874	molecular_function	ligase activity
L	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue COA A 601

Chain	Residue
A	ARG23
A	ARG30
A	PHE96
A	GLY129
A	TYR189

site_id	AC2
Number of Residues	8
Details	binding site for residue COA B 601

Chain	Residue
B	GLY129
B	ALA131
B	TYR189
B	ASP196
A	ILE438
B	ARG23
B	ARG30
B	PHE93

site_id	AC3
Number of Residues	3
Details	binding site for residue COA C 601

Chain	Residue
C	ARG30
C	PHE93
C	ALA131

site_id	AC4
Number of Residues	4
Details	binding site for residue COA D 601

Chain	Residue
D	ARG23
D	ARG30
D	GLY97
D	GLY129

site_id	AC5
Number of Residues	3
Details	binding site for residue COA E 601

Chain	Residue
E	ARG23
E	GLY129
E	ALA131

site_id	AC6
Number of Residues	5
Details	binding site for residue COA F 601

Chain	Residue
E	ILE438
F	ARG23
F	GLY129
F	ALA131
F	TYR189

site_id	AC7
Number of Residues	7
Details	binding site for Di-peptide BTI G 701 and LYS G 633

Chain	Residue
A	ASN278
A	PHE364
B	THR193
B	VAL201
G	GLU630
G	MET632
G	MET634

site_id	AC8
Number of Residues	7
Details	binding site for Di-peptide BTI H 701 and LYS H 633

Chain	Residue
C	ASN278
C	PHE364
D	THR193
H	GLU630
H	ALA631
H	MET632
H	MET634

site_id	AC9
Number of Residues	6
Details	binding site for Di-peptide BTI I 701 and LYS I 633

Chain	Residue
E	ASN278
E	PRO362
E	PHE364
I	ALA631
I	MET632
I	MET634

site_id	AD1
Number of Residues	8
Details	binding site for Di-peptide BTI J 701 and LYS J 633

Chain	Residue
A	THR193
A	VAL201
B	ASN278
B	PRO362
B	PHE364
J	ALA631
J	MET632
J	MET634

site_id	AD2
Number of Residues	6
Details	binding site for Di-peptide BTI K 701 and LYS K 633

Chain	Residue
F	ASN278
F	PHE364
K	GLU630
K	ALA631
K	MET632
K	MET634

site_id	AD3
Number of Residues	6
Details	binding site for Di-peptide BTI L 701 and LYS L 633

Chain	Residue
C	THR193
D	ASN278
D	PHE364
D	LYS433
L	MET632
L	MET634

Functional Information from PROSITE/UniProt

site_id	PS00188
Number of Residues	18
Details	BIOTIN Biotin-requiring enzymes attachment site. GEpLaiVeAMKMenvLrA

Chain	Residue	Details
G	GLY623-ALA640

site_id	PS00866
Number of Residues	15
Details	CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVMIKASaggGGkG

Chain	Residue	Details
G	TYR153-GLY167

site_id	PS00867
Number of Residues	8
Details	CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLEMNTRL

Chain	Residue	Details
G	PHE286-LEU293

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)