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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi68 – 681Copper
Metal bindingi106 – 1061Copper
Metal bindingi109 – 1091Copper
Metal bindingi114 – 1141Copper

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28281 PublicationAdd
BLAST
Chaini29 – 152124PseudoazurinPRO_0000002851Add
BLAST

Structurei

Secondary structure

1
152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 397Combined sources
Beta strandi42 – 5312Combined sources
Beta strandi58 – 625Combined sources
Beta strandi64 – 674Combined sources
Beta strandi92 – 954Combined sources
Beta strandi100 – 1056Combined sources
Turni107 – 1093Combined sources
Helixi110 – 1123Combined sources
Beta strandi115 – 1239Combined sources
Helixi127 – 1326Combined sources
Helixi137 – 14913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 29-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19567.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 12189Plastocyanin-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.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191Q → E AA sequence (PubMed:3595868).Curated

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
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. Positions 29-152.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP19567.

Family and domain databases

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...

Publicationsi

  1. "Cloning, characterization, and expression of the nitric oxide-generating nitrite reductase and of the blue copper protein genes of Achromobacter cycloclastes."
    Chen J.-Y., Chang W.-C., Chang T., Chang W.-C., Liu M.-Y., Payne W.J., le Gall J.
    Biochem. Biophys. Res. Commun. 219:423-428(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 21921 / IAM 1013.
  2. "The crystal structure of pseudoazurin from Alcaligenes faecalis S-6 determined at 2.9-A resolution."
    Petratos K., Banner D.W., Beppu T., Wilson K.S., Tsernoglou D.
    FEBS Lett. 218:209-214(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-152.
    Strain: ATCC 21921 / IAM 1013.
  3. "Crystallization and preliminary X-ray studies on pseudoazurin from Achromobacter cycloclastes IAM1013."
    Inoue T., Nishio N., Kai Y., Harada S., Ohshiro Y., Suzuki S., Kohzuma T., Shidara S., Iwasaki H.
    J. Biochem. 114:761-762(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).
    Strain: ATCC 21921 / IAM 1013.

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: June 8, 2016
This is version 102 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.