Cyanase C-terminal domain superfamily

SCOP classification

• Root: SCOP hierarchy in SUPERFAMILY [ 0] (11)
• Class: Alpha and beta proteins (a+b) [ 53931] (376)
• Fold: Cyanase C-terminal domain [ 55233]
• Superfamily: Cyanase C-terminal domain [ 55234]
• Families: Cyanase C-terminal domain [ 55235]

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Superfamily statistics

	Genomes (541)	Uniprot 2018_03 genome	PDB chains (SCOP 1.75)
Domains	606	4,197	3
Proteins	606	4,195	3

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Functional annotation

• General category: Metabolism
• Detailed category: Other enzymes

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Enzyme Commission (EC)

Highlighted in gray are those with FDR_all>0.001

	EC term	FDR (all)	IC level	SDEO level	Annotation (direct or inherited)
Enzyme Commission (EC)	Carbon-oxygen lyases	0	0.7274	--	DIRECT
Enzyme Commission (EC)	Cyanase	0	2.259	--	DIRECT
Enzyme Commission (EC)	Lyases	0	0.4169	Least Informative	DIRECT
Enzyme Commission (EC)	Hydro-lyases	0	0.8523	Moderately Informative	DIRECT

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Enzyme Commission (EC)

Highlighted in gray are those with FDR_all>0.001

	EC term	FDR (all)	IC level	SDEC level	Annotation (direct or inherited)
Enzyme Commission (EC)	Hydro-lyases	0	1.166	--	DIRECT
Enzyme Commission (EC)	Cyanase	0	2.651	--	DIRECT
Enzyme Commission (EC)	Lyases	0	0.6918	Least Informative	DIRECT
Enzyme Commission (EC)	Carbon-oxygen lyases	0	1.012	Moderately Informative	DIRECT

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UniProtKB KeyWords (KW)

Highlighted in gray are those with FDR_all>0.001

	KW term	FDR (all)	IC level	SDKW level	Annotation (direct or inherited)
Post-translational modification	Lyase	0	0.7634	Moderately Informative	DIRECT

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InterPro annotation

• Cross references: IPR003712 SSF55234 Protein matches
• Abstract: Some bacteria can overcome the toxicity of environmental cyanate by hydrolysis of cyanate. This reaction is catalyzed by cyanate lyase (also known as cyanase) [3049588]. Cyanate lyase is found in bacteria and plants and catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.

  The cyanate lyase monomer is composed of two domains. The N-terminal domain shows structural similarity to the DNA-binding alpha-helix bundle motif. The C-terminal domain has an 'open fold' with no structural homology to other proteins. The dimer structure reveals the C-terminal domains to be intertwined, and the decamer is formed by a pentamer of these dimers. The active site of the enzyme is located between dimers and is comprised of residues from four adjacent subunits of the homodecamer [10801492].

InterPro database

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