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
- Functionscopper ion binding / electron carrier activityProcessesoxidation-reduction processComponentsperiplasmic 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
- Copper-bind (PF00127)
- 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
Resource Link UniProtKB ID P22364 UniProtKB Entry Name AMCY_PARDE GenBank Gene ID X55665 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
- 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]
- Husain M, Davidson VL, Smith AJ: Properties of Paracoccus denitrificans amicyanin. Biochemistry. 1986 May 6;25(9):2431-6. [Article]
- 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]
- 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]
- 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]
- 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
Drug Drug group Pharmacological action? Type Actions Details L-methionine (S)-S-oxide experimental unknown target Details TRW3-(2-AMINO-3-HYDROXY-PROPYL)-6-(N'-CYCLOHEXYL-HYDRAZINO)OCTAHYDRO-INDOL-7-OL experimental unknown target Details