Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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...

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.