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Protein

Amicyanin

Gene

mauC

Organism
Paracoccus denitrificans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.

Cofactori

Cu cationNote: Binds 1 copper ion per subunit.

Pathwayi: methylamine degradation

This protein is involved in the pathway methylamine degradation, which is part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the pathway methylamine degradation and in One-carbon metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Copper
Metal bindingi118 – 1181Copper
Metal bindingi121 – 1211Copper
Metal bindingi124 – 1241Copper

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00895.

Names & Taxonomyi

Protein namesi
Recommended name:
Amicyanin
Gene namesi
Name:mauC
Synonyms:ami
OrganismiParacoccus denitrificans
Taxonomic identifieri266 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 131105AmicyaninPRO_0000002844Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiP22364. 3 interactions.

Structurei

Secondary structure

1
131
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 413Combined sources
Beta strandi47 – 526Combined sources
Beta strandi55 – 639Combined sources
Beta strandi68 – 736Combined sources
Beta strandi75 – 773Combined sources
Turni85 – 873Combined sources
Beta strandi88 – 914Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi112 – 1176Combined sources
Beta strandi125 – 1306Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AACX-ray1.31A27-131[»]
1AAJX-ray1.80A27-131[»]
1AANX-ray2.00A27-131[»]
1BXAX-ray1.30A27-131[»]
1MDAX-ray2.50A/B29-131[»]
1MG2X-ray2.25C/G/K/O27-131[»]
1MG3X-ray2.40C/G/K/O27-131[»]
1SF3X-ray1.05A27-131[»]
1SF5X-ray1.10A27-131[»]
1SFDX-ray0.99A/B27-131[»]
1SFHX-ray1.05A/B27-131[»]
1T5KX-ray1.40A/B/C/D27-131[»]
2GB2X-ray1.25A27-131[»]
2GBAX-ray0.92A27-131[»]
2GC4X-ray1.90C/G/K/O27-131[»]
2GC7X-ray1.90C/G/K/O27-131[»]
2IDQX-ray0.90A27-131[»]
2IDSX-ray1.00A27-131[»]
2IDTX-ray1.00A27-131[»]
2IDUX-ray0.95A27-131[»]
2J55X-ray2.15A/B27-131[»]
2J56X-ray2.10A/B27-131[»]
2J57X-ray2.25A/B/C/D27-131[»]
2MTAX-ray2.40A27-131[»]
2OV0X-ray0.75A27-131[»]
2QDVX-ray0.89A27-131[»]
2QDWX-ray0.92A27-131[»]
2RACX-ray1.30A27-131[»]
3IE9X-ray2.10A27-131[»]
3IEAX-ray2.20A27-131[»]
3L45Other1.80A27-131[»]
3PLYX-ray2.20A/B/C/D27-131[»]
3RYMX-ray1.70A/B/C/D27-131[»]
4P5RX-ray1.09A27-131[»]
4P5SX-ray1.02A27-131[»]
ProteinModelPortaliP22364.
SMRiP22364. Positions 27-131.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22364.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 131105Plastocyanin-likeAdd
BLAST

Sequence similaritiesi

Contains 1 plastocyanin-like domain.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR002386. Amicyanin/Pseudoazurin.
IPR013475. Amicyanin_precur.
IPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR001235. Copper_blue_Plastocyanin.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00127. Copper-bind. 1 hit.
[Graphical view]
PRINTSiPR00155. AMICYANIN.
PR00156. COPPERBLUE.
SUPFAMiSSF49503. SSF49503. 1 hit.
TIGRFAMsiTIGR02657. amicyanin. 1 hit.
PROSITEiPS00196. COPPER_BLUE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22364-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISATKIRSC LAACVLAAFG ATGALADKAT IPSESPFAAA EVADGAIVVD
60 70 80 90 100
IAKMKYETPE LHVKVGDTVT WINREAMPHN VHFVAGVLGE AALKGPMMKK
110 120 130
EQAYSLTFTE AGTYDYHCTP HPFMRGKVVV E
Length:131
Mass (Da):13,983
Last modified:August 1, 1991 - v1
Checksum:iF7352A865FD089DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55665 Genomic DNA. Translation: CAA39199.1.
PIRiA24407.
S12972.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55665 Genomic DNA. Translation: CAA39199.1.
PIRiA24407.
S12972.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AACX-ray1.31A27-131[»]
1AAJX-ray1.80A27-131[»]
1AANX-ray2.00A27-131[»]
1BXAX-ray1.30A27-131[»]
1MDAX-ray2.50A/B29-131[»]
1MG2X-ray2.25C/G/K/O27-131[»]
1MG3X-ray2.40C/G/K/O27-131[»]
1SF3X-ray1.05A27-131[»]
1SF5X-ray1.10A27-131[»]
1SFDX-ray0.99A/B27-131[»]
1SFHX-ray1.05A/B27-131[»]
1T5KX-ray1.40A/B/C/D27-131[»]
2GB2X-ray1.25A27-131[»]
2GBAX-ray0.92A27-131[»]
2GC4X-ray1.90C/G/K/O27-131[»]
2GC7X-ray1.90C/G/K/O27-131[»]
2IDQX-ray0.90A27-131[»]
2IDSX-ray1.00A27-131[»]
2IDTX-ray1.00A27-131[»]
2IDUX-ray0.95A27-131[»]
2J55X-ray2.15A/B27-131[»]
2J56X-ray2.10A/B27-131[»]
2J57X-ray2.25A/B/C/D27-131[»]
2MTAX-ray2.40A27-131[»]
2OV0X-ray0.75A27-131[»]
2QDVX-ray0.89A27-131[»]
2QDWX-ray0.92A27-131[»]
2RACX-ray1.30A27-131[»]
3IE9X-ray2.10A27-131[»]
3IEAX-ray2.20A27-131[»]
3L45Other1.80A27-131[»]
3PLYX-ray2.20A/B/C/D27-131[»]
3RYMX-ray1.70A/B/C/D27-131[»]
4P5RX-ray1.09A27-131[»]
4P5SX-ray1.02A27-131[»]
ProteinModelPortaliP22364.
SMRiP22364. Positions 27-131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP22364. 3 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00895.

Miscellaneous databases

EvolutionaryTraceiP22364.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR002386. Amicyanin/Pseudoazurin.
IPR013475. Amicyanin_precur.
IPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR001235. Copper_blue_Plastocyanin.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00127. Copper-bind. 1 hit.
[Graphical view]
PRINTSiPR00155. AMICYANIN.
PR00156. COPPERBLUE.
SUPFAMiSSF49503. SSF49503. 1 hit.
TIGRFAMsiTIGR02657. amicyanin. 1 hit.
PROSITEiPS00196. COPPER_BLUE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation."
    van Spanning R.J.M., Wansell C.W., Reijnders W.N.M., Oltmann L.F., Stouthamer A.H.
    FEBS Lett. 275:217-220(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 19367 / NBRC 13301 / NCIMB 8944 / NRRL B-3785.
  2. "Properties of Paracoccus denitrificans amicyanin."
    Husain M., Davidson V.L.
    Biochemistry 25:2431-2436(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-36.
  3. "Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin."
    Chen L., Durley R., Poliks B.J., Hamada K., Chen Z., Mathews F.S., Davidson V.L., Satow Y., Huizinga E.G., Vellieux F.M.D., Hol W.G.J.
    Biochemistry 31:4959-4964(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH MADH.
  4. "Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i."
    Chen L., Durley R., Mathews F.S., Davidson V.L.
    Science 264:86-90(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  5. "X-ray structure of the cupredoxin amicyanin, from Paracoccus denitrificans, refined at 1.31-A resolution."
    Cunane L.M., Chen Z.-W., Durley R.C.E., Mathews F.S.
    Acta Crystallogr. D 52:676-686(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.31 ANGSTROMS).
  6. "Molecular basis for interprotein complex-dependent effects on the redox properties of amicyanin."
    Zhu Z., Cunane L.M., Chen Z.-W., Durley R.C.E., Mathews F.S., Davidson V.L.
    Biochemistry 37:17128-17136(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), COPPER-BINDING SITES HIS-79; CYS-118; HIS-121 AND MET-124.

Entry informationi

Entry nameiAMCY_PARDE
AccessioniPrimary (citable) accession number: P22364
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 14, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.