2Z2A

Thr109Gly dihydroorotase from E. coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004151	molecular_function	dihydroorotase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
A	0006221	biological_process	pyrimidine nucleotide biosynthetic process
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A	0019856	biological_process	pyrimidine nucleobase biosynthetic process
A	0042803	molecular_function	protein homodimerization activity
A	0044205	biological_process	'de novo' UMP biosynthetic process
A	0046872	molecular_function	metal ion binding
B	0004151	molecular_function	dihydroorotase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
B	0006221	biological_process	pyrimidine nucleotide biosynthetic process
B	0008270	molecular_function	zinc ion binding
B	0016787	molecular_function	hydrolase activity
B	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B	0019856	biological_process	pyrimidine nucleobase biosynthetic process
B	0042803	molecular_function	protein homodimerization activity
B	0044205	biological_process	'de novo' UMP biosynthetic process
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 400

Chain	Residue
A	HIS16
A	HIS18
A	KCX102
A	ASP250
A	ZN401
A	HOH1411

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	ZN400
A	DOR1410
A	HOH1411
A	KCX102
A	HIS139
A	HIS177

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN B 400

Chain	Residue
B	HIS16
B	HIS18
B	KCX102
B	ASP250
B	ZN401
B	NCD2410
B	HOH2411

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN B 401

Chain	Residue
B	KCX102
B	HIS139
B	HIS177
B	ZN400
B	DOR1411
B	NCD2410
B	HOH2411

---

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE DOR A 1410

Chain	Residue
A	HIS18
A	ARG20
A	ASN44
A	HIS139
A	CYS221
A	LEU222
A	ASP250
A	ALA252
A	HIS254
A	ALA266
A	GLY267
A	ZN401
A	HOH1411
A	HOH1654
A	HOH1680

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DOR B 1411

Chain	Residue
B	HIS18
B	ARG20
B	ASN44
B	HIS139
B	CYS221
B	LEU222
B	ALA252
B	HIS254
B	ALA266
B	GLY267
B	ZN401
B	HOH2411

---

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NCD B 2410

Chain	Residue
B	HIS18
B	ARG20
B	ASN44
B	KCX102
B	HIS139
B	HIS177
B	CYS221
B	LEU222
B	ASP250
B	HIS254
B	ALA266
B	GLY267
B	ZN400
B	ZN401
B	HOH2411
B	HOH2668

---

Functional Information from PROSITE/UniProt

site_id	PS00482
Number of Residues	9
Details	DIHYDROOROTASE_1 Dihydroorotase signature 1. DWHLHLRdG

Chain	Residue	Details
A	ASP14-GLY22

---

site_id	PS00483
Number of Residues	12
Details	DIHYDROOROTASE_2 Dihydroorotase signature 2. GTDsAPHarhrK

Chain	Residue	Details
A	GLY248-LYS259

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000305|PubMed:15610022

Chain	Residue	Details
A	ASP250
B	ASP250

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651, ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE

Chain	Residue	Details
A	HIS16
B	ASP250
A	HIS18
A	HIS139
A	HIS177
A	ASP250
B	HIS16
B	HIS18
B	HIS139
B	HIS177

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000305|PubMed:11401542, ECO:0000305|PubMed:15826651, ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE

Chain	Residue	Details
A	ASN44
A	LEU222
A	HIS254
A	ALA266
B	ASN44
B	LEU222
B	HIS254
B	ALA266

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651, ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE

Chain	Residue	Details
A	KCX102
B	KCX102

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651, ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE

Chain	Residue	Details
A	KCX102
B	KCX102

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1j79

Chain	Residue	Details
A	ASP250

---

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1j79

Chain	Residue	Details
B	ASP250

---

site_id	MCSA1
Number of Residues	6
Details	M-CSA 630

Chain	Residue	Details
A	HIS16	metal ligand
A	HIS18	metal ligand
A	KCX102	metal ligand
A	HIS139	metal ligand
A	HIS177	metal ligand
A	ASP250	metal ligand, proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 630

Chain	Residue	Details
B	HIS16	metal ligand
B	HIS18	metal ligand
B	KCX102	metal ligand
B	HIS139	metal ligand
B	HIS177	metal ligand
B	ASP250	metal ligand, proton acceptor, proton donor

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