Amicyanin

Details

Name
Amicyanin
Kind
protein
Synonyms
  • ami
Gene Name
mauC
UniProtKB Entry
P22364Swiss-Prot
Organism
Paracoccus denitrificans
NCBI Taxonomy ID
266
Amino acid sequence
>lcl|BSEQ0011934|Amicyanin
MISATKIRSCLAACVLAAFGATGALADKATIPSESPFAAAEVADGAIVVDIAKMKYETPE
LHVKVGDTVTWINREAMPHNVHFVAGVLGEAALKGPMMKKEQAYSLTFTEAGTYDYHCTP
HPFMRGKVVVE
Number of residues
131
Molecular Weight
13983.11
Theoretical pI
6.67
GO Classification
Functions
copper ion binding / electron carrier activity
Processes
oxidation-reduction process
Components
periplasmic space
General Function
Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.
Specific Function
copper ion binding
Pfam Domain Function
Signal Regions
1-26
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0005382|396 bp
ATGATTTCTGCGACCAAGATCCGCTCGTGCCTGGCGGCCTGCGTCCTGGCGGCATTCGGC
GCGACGGGCGCCCTGGCCGACAAGGCGACGATCCCCTCGGAAAGCCCCTTTGCCGCCGCC
GAGGTGGCCGATGGCGCCATCGTCGTCGACATCGCCAAGATGAAATACGAAACCCCCGAA
CTTCATGTGAAGGTCGGCGACACCGTCACCTGGATCAACCGCGAGGCGATGCCGCACAAT
GTCCATTTCGTCGCCGGCGTGCTGGGCGAGGCGGCGTTGAAAGGCCCGATGATGAAGAAG
GAGCAGGCCTATTCCCTGACCTTCACCGAGGCCGGCACCTATGACTATCACTGCACCCCG
CATCCCTTCATGCGCGGCAAGGTCGTCGTCGAGTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP22364
UniProtKB Entry NameAMCY_PARDE
GenBank Gene IDX55665
PDB ID(s)1AAC, 1AAJ, 1AAN, 1BXA, 1MDA, 1MG2, 1MG3, 1SF3, 1SF5, 1SFD, 1SFH, 1T5K, 2GB2, 2GBA, 2GC4, 2GC7, 2IDQ, 2IDS, 2IDT, 2IDU, 2J55, 2J56, 2J57, 2MTA, 2OV0, 2QDV, 2QDW, 2RAC, 3IE9, 3IEA, 3L45, 3PLY, 3RYM, 4P5R, 4P5S
General References
  1. van Spanning RJ, Wansell CW, Reijnders WN, Oltmann LF, Stouthamer AH: Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation. FEBS Lett. 1990 Nov 26;275(1-2):217-20. [Article]
  2. Husain M, Davidson VL, Smith AJ: Properties of Paracoccus denitrificans amicyanin. Biochemistry. 1986 May 6;25(9):2431-6. [Article]
  3. Chen L, Durley R, Poliks BJ, Hamada K, Chen Z, Mathews FS, Davidson VL, Satow Y, Huizinga E, Vellieux FM, et al.: Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin. Biochemistry. 1992 Jun 2;31(21):4959-64. [Article]
  4. Chen L, Durley RC, Mathews FS, Davidson VL: Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i. Science. 1994 Apr 1;264(5155):86-90. [Article]
  5. Cunane LM, Chen ZW, Durley RC, Mathews FS: X-ray structure of the cupredoxin amicyanin, from Paracoccus denitrificans, refined at 1.31 A resolution. Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):676-86. [Article]
  6. Zhu Z, Cunane LM, Chen Z, Durley RC, Mathews FS, Davidson VL: Molecular basis for interprotein complex-dependent effects on the redox properties of amicyanin. Biochemistry. 1998 Dec 8;37(49):17128-36. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
L-methionine (S)-S-oxideexperimentalunknowntargetDetails
TRW3-(2-AMINO-3-HYDROXY-PROPYL)-6-(N'-CYCLOHEXYL-HYDRAZINO)OCTAHYDRO-INDOL-7-OLexperimentalunknowntargetDetails