Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1UPC

Carboxyethylarginine synthase from Streptomyces clavuligerus

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	0005948	cellular_component	acetolactate synthase complex
A	0009097	biological_process	isoleucine biosynthetic process
A	0009099	biological_process	valine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030976	molecular_function	thiamine pyrophosphate binding
A	0033848	molecular_function	N2-(2-carboxyethyl)arginine synthase activity
A	0046872	molecular_function	metal ion binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0003984	molecular_function	acetolactate synthase activity
B	0005948	cellular_component	acetolactate synthase complex
B	0009097	biological_process	isoleucine biosynthetic process
B	0009099	biological_process	valine biosynthetic process
B	0016740	molecular_function	transferase activity
B	0030976	molecular_function	thiamine pyrophosphate binding
B	0033848	molecular_function	N2-(2-carboxyethyl)arginine synthase activity
B	0046872	molecular_function	metal ion binding
B	0050660	molecular_function	flavin adenine dinucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0003984	molecular_function	acetolactate synthase activity
C	0005948	cellular_component	acetolactate synthase complex
C	0009097	biological_process	isoleucine biosynthetic process
C	0009099	biological_process	valine biosynthetic process
C	0016740	molecular_function	transferase activity
C	0030976	molecular_function	thiamine pyrophosphate binding
C	0033848	molecular_function	N2-(2-carboxyethyl)arginine synthase activity
C	0046872	molecular_function	metal ion binding
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0003984	molecular_function	acetolactate synthase activity
D	0005948	cellular_component	acetolactate synthase complex
D	0009097	biological_process	isoleucine biosynthetic process
D	0009099	biological_process	valine biosynthetic process
D	0016740	molecular_function	transferase activity
D	0030976	molecular_function	thiamine pyrophosphate binding
D	0033848	molecular_function	N2-(2-carboxyethyl)arginine synthase activity
D	0046872	molecular_function	metal ion binding
D	0050660	molecular_function	flavin adenine dinucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0003824	molecular_function	catalytic activity
E	0003984	molecular_function	acetolactate synthase activity
E	0005948	cellular_component	acetolactate synthase complex
E	0009097	biological_process	isoleucine biosynthetic process
E	0009099	biological_process	valine biosynthetic process
E	0016740	molecular_function	transferase activity
E	0030976	molecular_function	thiamine pyrophosphate binding
E	0033848	molecular_function	N2-(2-carboxyethyl)arginine synthase activity
E	0046872	molecular_function	metal ion binding
E	0050660	molecular_function	flavin adenine dinucleotide binding
F	0000287	molecular_function	magnesium ion binding
F	0003824	molecular_function	catalytic activity
F	0003984	molecular_function	acetolactate synthase activity
F	0005948	cellular_component	acetolactate synthase complex
F	0009097	biological_process	isoleucine biosynthetic process
F	0009099	biological_process	valine biosynthetic process
F	0016740	molecular_function	transferase activity
F	0030976	molecular_function	thiamine pyrophosphate binding
F	0033848	molecular_function	N2-(2-carboxyethyl)arginine synthase activity
F	0046872	molecular_function	metal ion binding
F	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 601

Chain	Residue
A	ASP463
A	ASN490
A	THR492
A	TPP600
A	HOH2121

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 602

Chain	Residue
A	HOH2068
A	HOH2106
A	HOH2139
B	HIS120
B	GLN121
A	TYR271
A	ARG414
A	HIS415
A	LEU495

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 603

Chain	Residue
A	ASN490
A	ASN560
A	TYR561
A	ASP562
A	PHE563

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 601

Chain	Residue
B	ASP463
B	ASN490
B	THR492
B	TPP600
B	HOH2182

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 B 602

Chain	Residue
A	HIS120
A	HOH2033
B	TYR271
B	ARG414
B	HIS415
B	LEU495
B	HOH2086
B	HOH2184
B	HOH2185

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 603

Chain	Residue
B	ASN490
B	ASN560
B	TYR561
B	ASP562
B	PHE563

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 601

Chain	Residue
C	ASP463
C	ASN490
C	THR492
C	TPP600
C	HOH2105

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 C 602

Chain	Residue
C	TYR271
C	ARG414
C	HIS415
C	HOH2067
C	HOH2116
C	HOH2118
D	HIS120
D	GLN121

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 603

Chain	Residue
C	ASN490
C	ASN560
C	TYR561
C	ASP562

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 601

Chain	Residue
D	ASP463
D	ASN490
D	THR492
D	TPP600
D	HOH2144

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 D 602

Chain	Residue
C	HIS120
C	GLN121
D	TYR271
D	ARG414
D	HIS415
D	LEU495
D	HOH2096
D	HOH2156
D	HOH2157

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 603

Chain	Residue
D	ASN490
D	ASN560
D	TYR561
D	ASP562

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 601

Chain	Residue
E	ASP463
E	ASN490
E	THR492
E	TPP600
E	HOH2110

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 E 602

Chain	Residue
E	TYR271
E	ARG414
E	HIS415
E	LEU495
E	HOH2076
F	HIS120
F	GLN121

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 603

Chain	Residue
E	ASN490
E	ASN560
E	TYR561
E	ASP562

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 601

Chain	Residue
F	ASP463
F	ASN490
F	THR492
F	TPP600
F	HOH2126

site_id	BC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 F 602

Chain	Residue
F	LEU495
F	HOH2064
F	HOH2136
E	HIS120
E	GLN121
F	TYR271
F	ARG414
F	HIS415

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F 603

Chain	Residue
F	ASN490
F	GLU497
F	ASN560
F	TYR561
F	ASP562

site_id	CC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TPP A 600

Chain	Residue
A	ILE410
A	GLY411
A	PHE412
A	PHE413
A	SER436
A	SER437
A	PHE438
A	GLY462
A	ASP463
A	GLY464
A	GLY465
A	ASN490
A	THR492
A	ASN493
A	GLY494
A	LEU495
A	TYR561
A	MG601
A	HOH2121
A	HOH2138
A	HOH2139
B	GLU57
B	THR80
B	ASN87

site_id	CC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TPP B 600

Chain	Residue
A	GLU57
A	THR80
A	ASN87
A	HOH2033
B	ILE410
B	GLY411
B	PHE412
B	PHE413
B	SER436
B	SER437
B	PHE438
B	GLY462
B	ASP463
B	GLY464
B	GLY465
B	ASN490
B	THR492
B	ASN493
B	GLY494
B	LEU495
B	TYR561
B	MG601
B	HOH2182
B	HOH2183

site_id	CC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TPP C 600

Chain	Residue
C	ILE410
C	GLY411
C	PHE412
C	PHE413
C	SER436
C	SER437
C	PHE438
C	GLY462
C	ASP463
C	GLY464
C	GLY465
C	ASN490
C	THR492
C	ASN493
C	GLY494
C	LEU495
C	TYR561
C	MG601
C	HOH2105
C	HOH2116
C	HOH2117
D	GLU57
D	THR80
D	ASN87

site_id	CC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TPP D 600

Chain	Residue
C	GLU57
C	THR80
C	ASN87
D	ILE410
D	GLY411
D	PHE412
D	PHE413
D	SER436
D	SER437
D	PHE438
D	GLY462
D	ASP463
D	GLY464
D	GLY465
D	ASN490
D	THR492
D	ASN493
D	GLY494
D	LEU495
D	TYR561
D	MG601
D	HOH2128
D	HOH2144
D	HOH2156

site_id	CC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE TPP E 600

Chain	Residue
E	ILE410
E	PHE412
E	PHE413
E	SER436
E	SER437
E	PHE438
E	GLY462
E	ASP463
E	GLY464
E	GLY465
E	ASN490
E	THR492
E	ASN493
E	GLY494
E	LEU495
E	TYR561
E	MG601
E	HOH2110
E	HOH2117
F	GLU57
F	THR80
F	ASN87

site_id	CC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE TPP F 600

Chain	Residue
E	GLU57
E	THR80
E	ASN87
F	ILE410
F	PHE412
F	PHE413
F	SER436
F	SER437
F	PHE438
F	GLY462
F	ASP463
F	GLY464
F	GLY465
F	ASN490
F	THR492
F	ASN493
F	GLY494
F	LEU495
F	TYR561
F	MG601
F	HOH2126
F	HOH2135

Functional Information from PROSITE/UniProt

site_id	PS00187
Number of Residues	20
Details	TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGaqmarPdqptFlIaGDGG

Chain	Residue	Details
A	ILE446-GLY465

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:19477162

Chain	Residue	Details
A	TYR271
C	ASP301
C	ARG414
C	LEU571
D	TYR271
D	ASP301
D	ARG414
D	LEU571
E	TYR271
E	ASP301
E	ARG414
A	ASP301
E	LEU571
F	TYR271
F	ASP301
F	ARG414
F	LEU571
A	ARG414
A	LEU571
B	TYR271
B	ASP301
B	ARG414
B	LEU571
C	TYR271

site_id	SWS_FT_FI2
Number of Residues	42
Details	BINDING: BINDING => ECO:0000269\|PubMed:14623876, ECO:0000269\|PubMed:19477162

Chain	Residue	Details
A	ILE410
B	ASP463
B	GLY464
B	ASN490
B	THR492
B	TYR561
C	ILE410
C	SER436
C	ASP463
C	GLY464
C	ASN490
A	SER436
C	THR492
C	TYR561
D	ILE410
D	SER436
D	ASP463
D	GLY464
D	ASN490
D	THR492
D	TYR561
E	ILE410
A	ASP463
E	SER436
E	ASP463
E	GLY464
E	ASN490
E	THR492
E	TYR561
F	ILE410
F	SER436
F	ASP463
F	GLY464
A	GLY464
F	ASN490
F	THR492
F	TYR561
A	ASN490
A	THR492
A	TYR561
B	ILE410
B	SER436

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
F	PRO565

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
A	PRO565

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
B	PRO565

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
C	PRO565

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
D	PRO565

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
E	PRO565

site_id	MCSA1
Number of Residues	6
Details	M-CSA 367

Chain	Residue	Details
A	GLU57	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	PHE438	steric role
A	ASP463	metal ligand
A	ASN490	metal ligand
A	THR492	metal ligand
A	TYR561	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA2
Number of Residues	6
Details	M-CSA 367

Chain	Residue	Details
B	GLU57	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	PHE438	steric role
B	ASP463	metal ligand
B	ASN490	metal ligand
B	THR492	metal ligand
B	TYR561	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA3
Number of Residues	6
Details	M-CSA 367

Chain	Residue	Details
C	GLU57	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	PHE438	steric role
C	ASP463	metal ligand
C	ASN490	metal ligand
C	THR492	metal ligand
C	TYR561	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA4
Number of Residues	6
Details	M-CSA 367

Chain	Residue	Details
D	GLU57	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	PHE438	steric role
D	ASP463	metal ligand
D	ASN490	metal ligand
D	THR492	metal ligand
D	TYR561	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA5
Number of Residues	6
Details	M-CSA 367

Chain	Residue	Details
E	GLU57	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	PHE438	steric role
E	ASP463	metal ligand
E	ASN490	metal ligand
E	THR492	metal ligand
E	TYR561	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA6
Number of Residues	6
Details	M-CSA 367

Chain	Residue	Details
F	GLU57	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	PHE438	steric role
F	ASP463	metal ligand
F	ASN490	metal ligand
F	THR492	metal ligand
F	TYR561	electrostatic stabiliser, hydrogen bond acceptor

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