6GDE

DIHYDROOROTASE FROM AQUIFEX AEOLICUS STANDARD (P,T)

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 500

Chain	Residue
A	HIS61
A	HIS63
A	ASP153
A	ASP305
A	HOH632

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP59-PRO67

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

Chain	Residue	Details
A	ALA303-LYS314

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00220

Chain	Residue	Details
A	ASP305

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:15826652, ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:1XRF, ECO:0007744|PDB:1XRT, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH

Chain	Residue	Details
A	HIS61
A	HIS63
A	ASP153

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:24314009, ECO:0007744|PDB:4BJH

Chain	Residue	Details
A	ASN95
A	ASN278
A	HIS309
A	PRO322

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH

Chain	Residue	Details
A	ASP305

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