Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00282 (AZUR_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. 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
Ordered Locus Names:PA4922
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length148 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.5 Ref.6
Chain21 – 148128Azurin
PRO_0000002863

Regions

Domain21 – 148128Plastocyanin-like

Sites

Metal binding661Copper Ref.13
Metal binding1321Copper Ref.13
Metal binding1371Copper Ref.13
Metal binding1411Copper

Amino acid modifications

Disulfide bond23 ↔ 46

Secondary structure

................................ 148
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00282 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 9C3881D7B6D64B67

FASTA14816,008
        10         20         30         40         50         60 
MLRKLAAVSL LSLLSAPLLA AECSVDIQGN DQMQFNTNAI TVDKSCKQFT VNLSHPGNLP 

        70         80         90        100        110        120 
KNVMGHNWVL STAADMQGVV TDGMASGLDK DYLKPDDSRV IAHTKLIGSG EKDSVTFDVS 

       130        140 
KLKEGEQYMF FCTFPGHSAL MKGTLTLK 

« Hide

References

« Hide 'large scale' references
[1]"The azurin gene from Pseudomonas aeruginosa. Cloning and characterization."
Arvidsson R.H.A., Nordling M., Lundberg L.G.
Eur. J. Biochem. 179:195-200(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10145 / DSM 50071 / JCM 5962 / LMG 1242 / NBRC 12689 / NCIMB 8295 / NRRL B-771.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a signal peptide. Cloning and sequencing of the azurin gene."
Canters G.W.
FEBS Lett. 212:168-172(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[5]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: PROTEIN SEQUENCE OF 21-148.
Strain: P6009.
[6]Charnock C.
Submitted (APR-1996) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 21-41.
Strain: ATCC 33352 / IATS 05.
[7]"A crystallographic model for azurin at 3-A resolution."
Adman E.T., Stenkamp R.E., Sieker L.C., Jensen L.H.
J. Mol. Biol. 123:35-47(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
[8]"Structural features of azurin at 2.7-A resolution."
Adman E.T., Jensen L.H.
Isr. J. Chem. 21:8-13(1981)
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[9]"Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85-A resolution."
Nar H., Messerschmidt A., Huber R., van de Kamp M., Canters G.W.
FEBS Lett. 306:119-124(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[10]"X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosa."
Hammann C., Messerschmidt A., Huber R., Nar H., Gilardi G., Canters G.W.
J. Mol. Biol. 255:362-366(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS SER-27 AND SER-130.
[11]"Crystal structures of modified apo-His117Gly and apo-His46Gly mutants of Pseudomonas aeruginosa azurin."
Hammann C., van Pouderoyen G., Nar H., Rueth F.-X.G., Messerschmidt A., Huber R., den Blaauwen T., Canters G.W.
J. Mol. Biol. 266:357-366(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT HIS-137.
[12]"X-ray structure determination and characterization of the Pseudomonas aeruginosa azurin mutant Met121Glu."
Karlsson B.G., Tsai L.-C., Nar H., Sanders-Loehr J., Bonander N., Langer V., Sjoelin L.
Biochemistry 36:4089-4095(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT GLU-141.
[13]"Complete sequential 1H and 15N nuclear magnetic resonance assignments and solution secondary structure of the blue copper protein azurin from Pseudomonas aeruginosa."
van de Kamp M., Canters G.W., Wijmenga S.S., Lommen A., Hilbers C.W., Nar H., Messerschmidt A., Huber R.
Biochemistry 31:10194-10207(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07317 Genomic DNA. Translation: CAA30279.1.
M30389 Genomic DNA. Translation: AAA25730.1.
AE004091 Genomic DNA. Translation: AAG08307.1.
PIRAZPSCA. JQ0644.
RefSeqNP_253609.1. NC_002516.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AG0X-ray2.40A/B20-148[»]
1AZNX-ray2.60A/B/C/D21-148[»]
1AZRX-ray2.40A/B/C/D21-148[»]
1AZUX-ray2.70A21-148[»]
1BEXX-ray2.30A/B21-148[»]
1CC3X-ray1.65A/B21-148[»]
1E5YX-ray2.00A/B/C/D21-148[»]
1E5ZX-ray2.00A/B/C/D21-148[»]
1E65X-ray1.85A/B/C/D21-148[»]
1E67X-ray2.14A/B/C/D21-148[»]
1ETJX-ray2.30A/B/C/D21-148[»]
1EZLX-ray2.00A/B/C/D21-148[»]
1GR7X-ray1.80A/B/C/D21-148[»]
1I53X-ray1.80A/B21-148[»]
1ILSX-ray2.20A/B/C/D21-148[»]
1ILUX-ray2.30A/B/C/D/E/F/G/H/I/K/L/M21-148[»]
1JVLX-ray2.00A/B21-148[»]
1JVOX-ray2.75A/B/C/D/E/F/G/H/I/J/K/L21-148[»]
1JZEX-ray1.60A21-148[»]
1JZFX-ray1.50A21-148[»]
1JZGX-ray1.40A21-148[»]
1JZHX-ray1.70A21-148[»]
1JZIX-ray1.62A/B21-148[»]
1JZJX-ray1.80A/B21-148[»]
1NZRX-ray2.20A/B/C/D21-148[»]
1R1CX-ray1.90A/B/C/D21-148[»]
1VLXX-ray1.90A/B/C/D21-148[»]
1XB3X-ray1.50A/B21-148[»]
1XB6X-ray1.82A/B21-148[»]
1XB8X-ray2.00A/C21-148[»]
2AZUX-ray1.90A/B/C/D21-148[»]
2FNWX-ray1.40A/B21-148[»]
2FT6X-ray1.25A21-148[»]
2FT7X-ray1.40A21-148[»]
2FT8X-ray1.55A21-148[»]
2FTAX-ray1.61A/B/C/D21-148[»]
2GHZX-ray1.60A/B21-148[»]
2GI0X-ray1.70A/B21-148[»]
2HX7X-ray1.55A/B21-148[»]
2HX8X-ray1.60A/B21-148[»]
2HX9X-ray1.70A/B21-148[»]
2HXAX-ray2.21A/B21-148[»]
2I7OX-ray1.50A21-148[»]
2I7SX-ray1.35A/B/C/D21-148[»]
2IDFX-ray2.25A/B21-148[»]
2IWEX-ray2.83A/D/G/J21-148[»]
2OJ1X-ray2.30A/B21-148[»]
2TSAX-ray2.20A/B/C/D21-148[»]
2TSBX-ray2.30A/B/C/D21-148[»]
2XV0X-ray1.60A21-148[»]
2XV2X-ray1.60A21-148[»]
2XV3X-ray2.30A/B21-148[»]
3AZUX-ray2.10A/B/C/D21-148[»]
3FPYX-ray2.10A21-148[»]
3FQ1X-ray1.90A21-148[»]
3FQ2X-ray1.91A21-148[»]
3FQYX-ray1.90A21-148[»]
3FS9X-ray1.05A21-132[»]
3FSAX-ray0.98A21-132[»]
3FSVX-ray2.30A21-132[»]
3FSWX-ray2.00A/B/C/D21-148[»]
3FSZX-ray2.00A/B21-132[»]
3FT0X-ray1.80A/B21-132[»]
3IBOX-ray1.45A/B/C/D21-148[»]
3IN0X-ray2.35A/B/C/D21-148[»]
3IN2X-ray2.60A21-148[»]
3JT2X-ray2.10A/B21-148[»]
3JTBX-ray1.80A/B/C/D21-148[»]
3N2JX-ray1.35A/B/C/D/E/F/G/H/I/J/K/L21-148[»]
3NP3X-ray2.10A21-148[»]
3NP4X-ray2.25A21-148[»]
3OQRX-ray2.40A21-148[»]
3U25X-ray1.18A/B22-148[»]
3UGEX-ray1.70A/B/C/D21-148[»]
4AZUX-ray1.90A/B/C/D21-148[»]
4HHGX-ray1.60A21-148[»]
4HHWX-ray2.00A/B21-148[»]
4HIPX-ray1.90A/B21-148[»]
4HZ1X-ray2.20A/B/C/D21-148[»]
4JKNX-ray1.54A/B/C/D21-148[»]
4K9JX-ray1.70A21-148[»]
4KO5X-ray1.79A/B21-148[»]
4KO6X-ray1.74A/B/C/D21-148[»]
4KO7X-ray2.07A/B/C/D21-148[»]
4KO9X-ray2.05A/B/C/D21-148[»]
4KOBX-ray1.87A/B/C/D21-148[»]
4KOCX-ray1.46A21-148[»]
4MFHX-ray1.54A/B/C21-148[»]
5AZUX-ray1.90A/B/C/D21-148[»]
ProteinModelPortalP00282.
SMRP00282. Positions 21-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48787N.
MINTMINT-8099376.
STRING208964.PA4922.

Protocols and materials databases

DNASU878046.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG08307; AAG08307; PA4922.
GeneID878046.
KEGGpae:PA4922.
PATRIC19844648. VBIPseAer58763_5155.

Organism-specific databases

PseudoCAPPA4922.

Phylogenomic databases

eggNOGCOG3241.
HOGENOMHOG000280572.
OMAESNDAMQ.
OrthoDBEOG6G20MV.
PhylomeDBP00282.

Family and domain databases

Gene3D2.60.40.420. 1 hit.
InterProIPR014068. Azurin_proteobac.
IPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamPF00127. Copper-bind. 1 hit.
[Graphical view]
SUPFAMSSF49503. SSF49503. 1 hit.
TIGRFAMsTIGR02695. azurin. 1 hit.
PROSITEPS00196. COPPER_BLUE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00282.

Entry information

Entry nameAZUR_PSEAE
AccessionPrimary (citable) accession number: P00282
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references