Azurin

Details

Name
Azurin
Synonyms
  • Azurin precursor
Gene Name
azu
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Amino acid sequence
>lcl|BSEQ0021295|Azurin
MLRKLAAVSLLSLLSAPLLAAECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLP
KNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVS
KLKEGEQYMFFCTFPGHSALMKGTLTLK
Number of residues
148
Molecular Weight
16008.315
Theoretical pI
6.93
GO Classification
Functions
copper ion binding / electron carrier activity / transition metal ion binding / zinc ion binding
Processes
oxidation-reduction process
Components
periplasmic space
General Function
Zinc ion binding
Specific Function
Transfers electrons from cytochrome c551 to cytochrome oxidase.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0021296|Azurin (azu)
ATGCTACGTAAACTCGCTGCGGTATCCCTGCTGTCCCTGCTCAGTGCGCCACTGCTGGCT
GCCGAGTGCTCGGTGGACATCCAGGGTAACGACCAGATGCAGTTCAACACCAATGCCATC
ACCGTCGACAAGAGCTGCAAGCAGTTCACCGTCAACCTGTCCCACCCCGGCAACCTGCCG
AAGAACGTCATGGGCCACAACTGGGTACTGAGCACCGCCGCCGACATGCAGGGCGTGGTC
ACCGACGGCATGGCTTCCGGCCTGGACAAGGATTACCTGAAGCCCGACGACAGCCGTGTC
ATCGCCCACACCAAGCTGATCGGCTCGGGCGAGAAGGACTCGGTGACCTTCGACGTCTCC
AAGCTGAAGGAAGGCGAGCAGTACATGTTCTTCTGCACCTTCCCGGGCCACTCCGCGCTG
ATGAAGGGCACCCTGACCCTGAAGTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00282
UniProtKB Entry NameAZUR_PSEAE
GenBank Protein ID45292
GenBank Gene IDX07317
General References
  1. Arvidsson RH, Nordling M, Lundberg LG: The azurin gene from Pseudomonas aeruginosa. Cloning and characterization. Eur J Biochem. 1989 Jan 15;179(1):195-200. [Article]
  2. Hoitink CW, Woudt LP, Turenhout JC, van de Kamp M, Canters GW: Isolation and sequencing of the Alcaligenes denitrificans azurin-encoding gene: comparison with the genes encoding blue copper proteins from Pseudomonas aeruginosa and Alcaligenes faecalis. Gene. 1990 May 31;90(1):15-20. [Article]
  3. Canters GW: The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a signal peptide. Cloning and sequencing of the azurin gene. FEBS Lett. 1987 Feb 9;212(1):168-72. [Article]
  4. Stover CK, Pham XQ, Erwin AL, Mizoguchi SD, Warrener P, Hickey MJ, Brinkman FS, Hufnagle WO, Kowalik DJ, Lagrou M, Garber RL, Goltry L, Tolentino E, Westbrock-Wadman S, Yuan Y, Brody LL, Coulter SN, Folger KR, Kas A, Larbig K, Lim R, Smith K, Spencer D, Wong GK, Wu Z, Paulsen IT, Reizer J, Saier MH, Hancock RE, Lory S, Olson MV: Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature. 2000 Aug 31;406(6799):959-64. [Article]
  5. Adman ET, Stenkamp RE, Sieker LC, Jensen LH: A crystallographic model for azurin a 3 A resolution. J Mol Biol. 1978 Jul 25;123(1):35-47. [Article]
  6. Nar H, Messerschmidt A, Huber R, van de Kamp M, Canters GW: Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 A resolution. FEBS Lett. 1992 Jul 20;306(2-3):119-24. [Article]
  7. Hammann C, Messerschmidt A, Huber R, Nar H, Gilardi G, Canters GW: X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosa. J Mol Biol. 1996 Jan 26;255(3):362-6. [Article]
  8. Hammann C, van Pouderoyen G, Nar H, Gomis Ruth FX, Messerschmidt A, Huber R, den Blaauwen T, Canters GW: Crystal structures of modified apo-His117Gly and apo-His46Gly mutants of Pseudomonas aeruginosa azurin. J Mol Biol. 1997 Feb 21;266(2):357-66. [Article]
  9. Karlsson BG, Tsai LC, Nar H, Sanders-Loehr J, Bonander N, Langer V, Sjolin L: X-ray structure determination and characterization of the Pseudomonas aeruginosa azurin mutant Met121Glu. Biochemistry. 1997 Apr 8;36(14):4089-95. [Article]
  10. van de Kamp M, Canters GW, Wijmenga SS, Lommen A, Hilbers CW, Nar H, Messerschmidt A, Huber R: Complete sequential 1H and 15N nuclear magnetic resonance assignments and solution secondary structure of the blue copper protein azurin from Pseudomonas aeruginosa. Biochemistry. 1992 Oct 27;31(42):10194-207. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01915S-HydroxycysteineexperimentalunknownDetails
DB025864,7-Dimethyl-[1,10]PhenanthrolineexperimentalunknownDetails
DB03492lambda-bis(2,2'-bipyridine)imidazole osmium (II)experimentalunknownDetails
DB03570Tris-Hydroxymethyl-Methyl-AmmoniumexperimentalunknownDetails
DB03840Tetra(Imidazole)Diaquacopper (Ii)experimentalunknownDetails
DB03871lambda-bis(2,2'-bipyridine)imidazole ruthenium (II)experimentalunknownDetails
DB04085Bis(N-maleimidomethyl)etherexperimentalunknownDetails
DB04100Tricarbonyl(1,10-phenanthroline)rhenium(1+)experimentalunknownDetails
DB04231Tetra(imidazole)diaquacopper (I)experimentalunknownDetails
DB069681,1'-HEXANE-1,6-DIYLBIS(1H-IMIDAZOLE)experimentalunknownDetails