4YIW

DIHYDROOROTASE FROM BACILLUS ANTHRACIS WITH SUBSTRATE BOUND

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004038	molecular_function	allantoinase activity
A	0004151	molecular_function	dihydroorotase activity
A	0005737	cellular_component	cytoplasm
A	0006145	biological_process	purine nucleobase catabolic process
A	0006221	biological_process	pyrimidine nucleotide biosynthetic process
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A	0044205	biological_process	'de novo' UMP biosynthetic process
A	0046872	molecular_function	metal ion binding
B	0004038	molecular_function	allantoinase activity
B	0004151	molecular_function	dihydroorotase activity
B	0005737	cellular_component	cytoplasm
B	0006145	biological_process	purine nucleobase catabolic process
B	0006221	biological_process	pyrimidine nucleotide biosynthetic process
B	0008270	molecular_function	zinc ion binding
B	0016787	molecular_function	hydrolase activity
B	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
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 501

Chain	Residue
A	HIS59
A	HIS61
A	ASP151
A	ASP304
A	ZN502
A	NCD503

---

site_id	AC2
Number of Residues	5
Details	binding site for residue ZN A 502

Chain	Residue
A	ZN501
A	NCD503
A	ASP151
A	HIS178
A	HIS231

---

site_id	AC3
Number of Residues	11
Details	binding site for residue NCD A 503

Chain	Residue
A	HIS61
A	ARG63
A	ASN93
A	MET276
A	ASN277
A	ASP304
A	HIS308
A	PHE322
A	GLY323
A	ZN501
A	ZN502

---

site_id	AC4
Number of Residues	6
Details	binding site for residue ZN B 501

Chain	Residue
B	HIS59
B	HIS61
B	ASP151
B	ASP304
B	ZN502
B	NCD503

---

site_id	AC5
Number of Residues	5
Details	binding site for residue ZN B 502

Chain	Residue
B	ASP151
B	HIS178
B	HIS231
B	ZN501
B	NCD503

---

site_id	AC6
Number of Residues	14
Details	binding site for residue NCD B 503

Chain	Residue
B	HIS61
B	ARG63
B	ASN93
B	GLY152
B	HIS178
B	MET276
B	ASN277
B	ASP304
B	ALA306
B	HIS308
B	PHE322
B	GLY323
B	ZN501
B	ZN502

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP57-PRO65

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

Chain	Residue	Details
A	ALA302-LYS313

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:27499369

Chain	Residue	Details
A	ASP304
B	ASP304

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000269|PubMed:21045288, ECO:0000269|PubMed:27499369, ECO:0007744|PDB:3MPG, ECO:0007744|PDB:4YIW

Chain	Residue	Details
A	HIS59
B	HIS178
B	HIS231
B	ASP304
A	HIS61
A	ASP151
A	HIS178
A	HIS231
A	ASP304
B	HIS59
B	HIS61
B	ASP151

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:27499369

Chain	Residue	Details
A	ASN93
A	ASN277
A	HIS308
A	PHE322
B	ASN93
B	ASN277
B	HIS308
B	PHE322

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