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P00280 (AZUR_ALCDE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Azurin
Gene names
Name:azu
OrganismAlcaligenes denitrificans (Achromobacter denitrificans)
Taxonomic identifier32002 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAchromobacter

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transfers electrons from cytochrome c551 to cytochrome oxidase.

Subcellular location

Periplasm.

Sequence similarities

Contains 1 plastocyanin-like domain.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentPeriplasm
   DomainSignal
   LigandCopper
Metal-binding
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.2
Chain21 – 149129Azurin
PRO_0000002858

Regions

Domain21 – 149129Plastocyanin-like

Sites

Metal binding661Copper Ref.5
Metal binding1321Copper Ref.5
Metal binding1371Copper Ref.5
Metal binding1411Copper Ref.5

Amino acid modifications

Disulfide bond23 ↔ 46

Experimental info

Sequence conflict771Q → E AA sequence Ref.2

Secondary structure

........................... 149
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00280 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 849F182DD6B1BE3B

FASTA14915,924
        10         20         30         40         50         60 
MLAKATLAIV LSAASLPVLA AQCEATIESN DAMQYNLKEM VVDKSCKQFT VHLKHVGKMA 

        70         80         90        100        110        120 
KVAMGHNWVL TKEADKQGVA TDGMNAGLAQ DYVKAGDTRV IAHTKVIGGG ESDSVTFDVS 

       130        140 
KLTPGEAYAY FCSFPGHWAM MKGTLKLSN 

« Hide

References

[1]"Isolation and sequencing of the Alcaligenes denitrificans azurin-encoding gene: comparison with the genes encoding blue copper proteins from Pseudomonas aeruginosa and Alcaligenes faecalis."
Hoitink C.W.G., Woudt L.P., Turenhout J.C.M., van de Kamp M., Canters G.W.
Gene 90:15-20(1990) [PubMed: 2116366] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Ambler R.P.
Submitted (DEC-1974) to the PIR data bank
Cited for: PROTEIN SEQUENCE OF 21-149.
Strain: ATCC 15173 / DSM 30026 / JCM 5490 / NBRC 15125 / NCIMB 11961 / NCTC 8582.
[3]Ambler R.P.
(In) Preverio A., Pechere J.-F., Coletti-preverio M.-A. (eds.); Developpements recents dans l'etude chimique de la structure des proteines, pp.289-305, INSERM, Paris (1971)
Cited for: PARTIAL PROTEIN SEQUENCE.
[4]"Structure of azurin from Alcaligenes denitrificans at 2.5-A resolution."
Norris G.E., Anderson B.F., Baker E.N.
J. Mol. Biol. 165:501-521(1983) [PubMed: 6842609] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]"Structure of azurin from Alcaligenes denitrificans refinement at 1.8-A resolution and comparison of the two crystallographically independent molecules."
Baker E.N.
J. Mol. Biol. 203:1071-1095(1988) [PubMed: 3210236] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[6]"X-ray analysis and spectroscopic characterization of M121Q azurin. A copper site model for stellacyanin."
Romero A., Hoitink C.W., Nar H., Huber R., Messerschmidt A., Canters G.W.
J. Mol. Biol. 229:1007-1021(1993) [PubMed: 8383207] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF GLN-141.
[7]"Paramagnetic cobalt and nickel derivatives of Alcaligenes denitrificans azurin and its M121Q mutant. A 1H NMR study."
Kroes S., Wamerdam G.C.M., Canters G.W.
Biochemistry 35:1810-1819(1996) [PubMed: 8639662] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M30388 Genomic DNA. Translation: AAA21954.1.
PIRAZALCD. JQ0643.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4AX-ray1.89A/B21-149[»]
1A4BX-ray1.91A/B21-149[»]
1A4CX-ray2.45A/B/C/D21-149[»]
1AIZX-ray1.80A/B21-149[»]
1AZBX-ray2.20A/B21-149[»]
1AZCX-ray1.80A/B21-149[»]
1URIX-ray1.94A/B21-149[»]
2AZAX-ray1.80A/B21-149[»]
ProteinModelPortalP00280.
SMRP00280. Positions 21-149.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR014068. Azurin_proteobac.
IPR000923. BlueCu_1.
IPR008972. Cupredoxin.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 1 hit.
PfamPF00127. Copper-bind. 1 hit.
[Graphical view]
SUPFAMSSF49503. Cupredoxin. 1 hit.
TIGRFAMsTIGR02695. Azurin. 1 hit.
PROSITEPS00196. COPPER_BLUE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAZUR_ALCDE
AccessionPrimary (citable) accession number: P00280
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: May 31, 2011
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families