Literature summary for 7.6.2.2 extracted from

Shukla, S.; Rai, V.; Banerjee, D.; Prasad, R.
Characterization of Cdr1p, a major multidrug efflux protein of Candida albicans: purified protein is amenable to intrinsic fluorescence analysis (2006), Biochemistry, 45, 2425-2435.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
plasma membrane	-	Candida albicans	5886	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	divalent cation required in the order of descending efficiency: Mg2+, Mn2+, Ca2+, Co2+	Candida albicans
Co2+	divalent cation required in the order of descending efficiency: Mg2+, Mn2+, Ca2+, Co2+	Candida albicans
Mg2+	divalent cation required in the order of descending efficiency: Mg2+, Mn2+, Ca2+, Co2+	Candida albicans
Mn2+	divalent cation required in the order of descending efficiency: Mg2+, Mn2+, Ca2+, Co2+	Candida albicans

Organism

Organism	UniProt	Comment	Textmining
Candida albicans	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Candida albicans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	ATP binding to Cdr1p is not a prerequisite for drug binding and both drug as well as ATP binding, which induce specific conformational changes, can occur independently of each other	Candida albicans	ADP + phosphate	-	?
CTP + H2O	-	Candida albicans	CDP + phosphate	-	?
GTP + H2O	-	Candida albicans	GDP + phosphate	-	?
UTP + H2O	-	Candida albicans	UDP + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
Cdr1p	-	Candida albicans

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Release 2023.1 (January 2023)