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Protein

Amicyanin

Gene

mauC

Organism
Paracoccus versutus (Thiobacillus versutus)
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi80 – 801Copper
Metal bindingi119 – 1191Copper
Metal bindingi122 – 1221Copper
Metal bindingi125 – 1251Copper

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 versutus (Thiobacillus versutus)
Taxonomic identifieri34007 [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 – 132106AmicyaninPRO_0000002845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271Pyrrolidone carboxylic acid

Keywords - PTMi

Pyrrolidone carboxylic acid

Structurei

Secondary structure

1
132
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 313Combined sources
Helixi40 – 423Combined sources
Beta strandi48 – 536Combined sources
Beta strandi56 – 649Combined sources
Beta strandi69 – 746Combined sources
Beta strandi76 – 783Combined sources
Beta strandi88 – 925Combined sources
Beta strandi103 – 1097Combined sources
Beta strandi113 – 1186Combined sources
Beta strandi126 – 1316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ID2X-ray2.15A/B/C27-132[»]
3C75X-ray2.50A/B1-132[»]
ProteinModelPortaliP22365.
SMRiP22365. Positions 27-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22365.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 132106Plastocyanin-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.

P22365-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISAKTLRPA IAAIALFAIG ATGAWAQDKI TVTSEKPVAA ADVPADAVVV
60 70 80 90 100
GIEKMKYLTP EVTIKAGETV YWVNGEVMPH NVAFKKGIVG EDAFRGEMMT
110 120 130
KDQAYAITFN EAGSYDYFCT PHPFMRGKVI VE
Length:132
Mass (Da):14,259
Last modified:October 1, 1996 - v3
Checksum:i2E64C930BD18C41D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58001 Genomic DNA. Translation: AAA50571.1.
PIRiS19732. A23706.
RefSeqiWP_036750422.1. NZ_JRKO01000005.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58001 Genomic DNA. Translation: AAA50571.1.
PIRiS19732. A23706.
RefSeqiWP_036750422.1. NZ_JRKO01000005.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ID2X-ray2.15A/B/C27-132[»]
3C75X-ray2.50A/B1-132[»]
ProteinModelPortaliP22365.
SMRiP22365. Positions 27-132.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00895.

Miscellaneous databases

EvolutionaryTraceiP22365.

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. "Cloning, sequencing and expression studies of the genes encoding amicyanin and the beta-subunit of methylamine dehydrogenase from Thiobacillus versutus."
    Ubbink M., van Kleef M.A., Kleinjan D.J., Hoitink C.W., Huitema F., Beintema J.J., Duine J.A., Canters G.W.
    Eur. J. Biochem. 202:1003-1012(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The structural homology of amicyanin from Thiobacillus versutus to plant plastocyanins."
    van Beeumen J., van Bun S., Canters G.W., Lommen A., Chothia C.
    J. Biol. Chem. 266:4869-4877(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-132.
  3. "Crystal structure analysis and refinement at 2.15-A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus."
    Romero A., Nar H., Huber R., Messerchmidt A., Kalverda A.P., Canters G.W., Durley R., Mathews F.S.
    J. Mol. Biol. 236:1196-1211(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
  4. "Assignment of the 600-MHz 1H-NMR spectrum of amicyanin from Thiobacillus versutus by two-dimensional NMR methods provides information on secondary structure."
    Lommen A., Wijmenga S., Jilbers C.W., Canters G.W.
    Eur. J. Biochem. 201:695-702(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  5. "Solution structure of the type 1 blue copper protein amicyanin from Thiobacillus versutus."
    Kalverda A.P., Wymenga S.S., Lommen A., van de Ven F.J.M., Hilbers C.W., Canters G.W.
    J. Mol. Biol. 240:358-371(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  6. "A 1H NMR study of the paramagnetic active site of the CuA variant of amicyanin."
    Dennison C., Berg A., Canters G.W.
    Biochemistry 36:3262-3269(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiAMCY_PARVE
AccessioniPrimary (citable) accession number: P22365
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 1, 1996
Last modified: December 9, 2015
This is version 103 of the entry and version 3 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.