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Protein

Pseudoazurin

Gene

bcp

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

Functioni

This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen.

Cofactori

Cu cationNote: Binds 1 copper ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi68Copper1
Metal bindingi106Copper1
Metal bindingi109Copper1
Metal bindingi114Copper1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Pseudoazurin
Alternative name(s):
Blue copper protein
Gene namesi
Name:bcp
OrganismiAchromobacter cycloclastes
Taxonomic identifieri223 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAchromobacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 281 PublicationAdd BLAST28
ChainiPRO_000000285129 – 152PseudoazurinAdd BLAST124

Structurei

Secondary structure

1152
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 39Combined sources7
Beta strandi42 – 53Combined sources12
Beta strandi58 – 62Combined sources5
Beta strandi64 – 67Combined sources4
Beta strandi92 – 95Combined sources4
Beta strandi100 – 105Combined sources6
Turni107 – 109Combined sources3
Helixi110 – 112Combined sources3
Beta strandi115 – 123Combined sources9
Helixi127 – 132Combined sources6
Helixi137 – 149Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BQKX-ray1.35A29-152[»]
1BQRX-ray1.60A29-152[»]
1ZIAX-ray1.54A29-152[»]
1ZIBX-ray2.00A29-152[»]
2JKWX-ray1.60A/B29-152[»]
2UX6X-ray1.30A29-152[»]
2UX7X-ray1.30A29-152[»]
2UXFX-ray2.00A29-152[»]
2UXGX-ray1.99A29-152[»]
4YL4X-ray1.10A29-152[»]
ProteinModelPortaliP19567.
SMRiP19567.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19567.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 121Plastocyanin-likeAdd BLAST89

Sequence similaritiesi

Contains 1 plastocyanin-like domain.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd04218. Pseudoazurin. 1 hit.
Gene3Di2.60.40.420. 1 hit.
InterProiIPR002386. Amicyanin/Pseudoazurin.
IPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR001235. Copper_blue_Plastocyanin.
IPR008972. Cupredoxin.
IPR012745. Pseudoazurin.
[Graphical view]
PfamiPF00127. Copper-bind. 1 hit.
[Graphical view]
PRINTSiPR00155. AMICYANIN.
PR00156. COPPERBLUE.
SUPFAMiSSF49503. SSF49503. 1 hit.
TIGRFAMsiTIGR02375. pseudoazurin. 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.

P19567-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKTMLNAIK SGFGIAIAAM LVAAPAAAAD FEVHMLNKGK DGAMVFEPAS
60 70 80 90 100
LKVAPGDTVT FIPTDKGHNV ETIKGMIPDG AEAFKSKINE NYKVTFTAPG
110 120 130 140 150
VYGVKCTPHY GMGMVGVVQV GDAPANLEAV KGAKNPKKAQ ERLDAALAAL

GN
Length:152
Mass (Da):15,760
Last modified:November 1, 1997 - v2
Checksum:i732F736DE38506D1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti119Q → E AA sequence (PubMed:3595868).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48669 Genomic DNA. Translation: CAA88588.1.
PIRiJC4649.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48669 Genomic DNA. Translation: CAA88588.1.
PIRiJC4649.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BQKX-ray1.35A29-152[»]
1BQRX-ray1.60A29-152[»]
1ZIAX-ray1.54A29-152[»]
1ZIBX-ray2.00A29-152[»]
2JKWX-ray1.60A/B29-152[»]
2UX6X-ray1.30A29-152[»]
2UX7X-ray1.30A29-152[»]
2UXFX-ray2.00A29-152[»]
2UXGX-ray1.99A29-152[»]
4YL4X-ray1.10A29-152[»]
ProteinModelPortaliP19567.
SMRiP19567.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP19567.

Family and domain databases

CDDicd04218. Pseudoazurin. 1 hit.
Gene3Di2.60.40.420. 1 hit.
InterProiIPR002386. Amicyanin/Pseudoazurin.
IPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR001235. Copper_blue_Plastocyanin.
IPR008972. Cupredoxin.
IPR012745. Pseudoazurin.
[Graphical view]
PfamiPF00127. Copper-bind. 1 hit.
[Graphical view]
PRINTSiPR00155. AMICYANIN.
PR00156. COPPERBLUE.
SUPFAMiSSF49503. SSF49503. 1 hit.
TIGRFAMsiTIGR02375. pseudoazurin. 1 hit.
PROSITEiPS00196. COPPER_BLUE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAZUP_ACHCY
AccessioniPrimary (citable) accession number: P19567
Secondary accession number(s): Q43929
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 104 of the entry and version 2 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.