Azurin precursor - Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)

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P00282 (AZUR_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 127. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Azurin

Gene names

Name:	azu
Ordered Locus Names:	PA4922

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length	148 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Electron transport Transport
Cellular component	Periplasm
Domain	Signal
Ligand	Copper Metal-binding
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Ref.5 Ref.6

Chain

21 – 148

128

Azurin

PRO_0000002863

Regions

Domain

21 – 148

128

Plastocyanin-like

Sites

Metal binding

Copper Ref.13

Metal binding

132

Copper Ref.13

Metal binding

137

Copper Ref.13

Metal binding

141

Copper

Amino acid modifications

Disulfide bond

23 ↔ 46

Secondary structure

148

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00282 [UniParc].

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

FASTA

148

16,008

        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' referencesShow '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. 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.

PIR

AZPSCA. JQ0644.

RefSeq

NP_253609.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AG0	X-ray	2.40	A/B	20-148	[»]
1AZN	X-ray	2.60	A/B/C/D	21-148	[»]
1AZR	X-ray	2.40	A/B/C/D	23-148	[»]
1AZU	X-ray	2.70	A	21-148	[»]
1BEX	X-ray	2.30	A/B	21-148	[»]
1CC3	X-ray	1.65	A/B	21-148	[»]
1E5Y	X-ray	2.00	A/B/C/D	21-148	[»]
1E5Z	X-ray	2.00	A/B/C/D	21-148	[»]
1E65	X-ray	1.85	A/B/C/D	21-148	[»]
1E67	X-ray	2.14	A/B/C/D	21-148	[»]
1ETJ	X-ray	2.30	A/B/C/D	21-148	[»]
1EZL	X-ray	2.00	A/B/C/D	21-148	[»]
1GR7	X-ray	1.80	A/B/C/D	21-148	[»]
1I53	X-ray	1.80	A/B	23-148	[»]
1ILS	X-ray	2.20	A/B/C/D	21-148	[»]
1ILU	X-ray	2.30	A/B/C/D/E/F/G/H/I/K/L/M	21-148	[»]
1JVL	X-ray	2.00	A/B	21-148	[»]
1JVO	X-ray	2.75	A/B/C/D/E/F/G/H/I/J/K/L	21-148	[»]
1JZE	X-ray	1.60	A	21-148	[»]
1JZF	X-ray	1.50	A	21-148	[»]
1JZG	X-ray	1.40	A	21-148	[»]
1JZH	X-ray	1.70	A	21-148	[»]
1JZI	X-ray	1.62	A/B	21-148	[»]
1JZJ	X-ray	1.80	A/B	21-148	[»]
1NZR	X-ray	2.20	A/B/C/D	21-148	[»]
1R1C	X-ray	1.90	A/B/C/D	21-148	[»]
1VLX	X-ray	1.90	A/B/C/D	21-148	[»]
1XB3	X-ray	1.50	A/B	21-148	[»]
1XB6	X-ray	1.82	A/B	21-148	[»]
1XB8	X-ray	2.00	A/C	21-148	[»]
2AZU	X-ray	1.90	A/B/C/D	23-148	[»]
2FNW	X-ray	1.40	A/B	23-148	[»]
2FT6	X-ray	1.25	A	21-133	[»]
2FT7	X-ray	1.40	A	21-133	[»]
2FT8	X-ray	1.55	A	21-133	[»]
2FTA	X-ray	1.61	A/B/C/D	21-133	[»]
2GHZ	X-ray	1.60	A/B	21-148	[»]
2GI0	X-ray	1.70	A/B	21-148	[»]
2HX7	X-ray	1.55	A/B	21-132	[»]
2HX8	X-ray	1.60	A/B	21-132	[»]
2HX9	X-ray	1.70	A/B	21-132	[»]
2HXA	X-ray	2.21	A/B	21-132	[»]
2I7O	X-ray	1.50	A	23-148	[»]
2I7S	X-ray	1.35	A/B/C/D	23-148	[»]
2IDF	X-ray	2.25	A/B	21-148	[»]
2IWE	X-ray	2.83	A/D/G/J	21-148	[»]
2OJ1	X-ray	2.30	A/B	21-148	[»]
2TSA	X-ray	2.20	A/B/C/D	21-148	[»]
2TSB	X-ray	2.30	A/B/C/D	21-148	[»]
2XV0	X-ray	1.60	A	21-132	[»]
2XV2	X-ray	1.60	A	21-132	[»]
2XV3	X-ray	2.30	A/B	21-132	[»]
3AZU	X-ray	2.10	A/B/C/D	23-148	[»]
3FPY	X-ray	2.10	A	21-148	[»]
3FQ1	X-ray	1.90	A	21-148	[»]
3FQ2	X-ray	1.91	A	21-148	[»]
3FQY	X-ray	1.90	A	21-148	[»]
3FS9	X-ray	1.05	A	21-132	[»]
3FSA	X-ray	0.98	A	21-132	[»]
3FSV	X-ray	2.30	A	21-132	[»]
3FSW	X-ray	2.00	A/B/C/D	21-148	[»]
3FSZ	X-ray	2.00	A/B	21-132	[»]
3FT0	X-ray	1.80	A/B	21-132	[»]
3IBO	X-ray	1.45	A/B/C/D	23-148	[»]
3IN0	X-ray	2.35	A/B/C/D	21-148	[»]
3IN2	X-ray	2.60	A	21-148	[»]
3JT2	X-ray	2.10	A/B	21-148	[»]
3JTB	X-ray	1.80	A/B/C/D	21-148	[»]
3N2J	X-ray	1.35	A/B/C/D/E/F/G/H/I/J/K/L	21-148	[»]
3NP3	X-ray	2.10	A	21-148	[»]
3NP4	X-ray	2.25	A	21-148	[»]
3OQR	X-ray	2.40	A	21-148	[»]
3U25	X-ray	1.18	A/B	22-148	[»]
3UGE	X-ray	1.70	A/B/C/D	21-148	[»]
4AZU	X-ray	1.90	A/B/C/D	21-148	[»]
4HHG	X-ray	1.60	A	21-148	[»]
4HHW	X-ray	2.00	A/B	21-148	[»]
4HIP	X-ray	1.90	A/B	21-148	[»]
4HZ1	X-ray	2.20	A/B/C/D	21-148	[»]
5AZU	X-ray	1.90	A/B/C/D	21-148	[»]

ProteinModelPortal

P00282.

SMR

P00282. Positions 21-148.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48787N.

MINT

MINT-8099376.

STRING

208964.PA4922.

Protocols and materials databases

DNASU

878046.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

878046.

KEGG

pae:PA4922.

PATRIC

19844648. VBIPseAer58763_5155.

Organism-specific databases

PseudoCAP

PA4922.

Phylogenomic databases

eggNOG

COG3241.

HOGENOM

HOG000280572.

OMA

TDGMAAG.

ProtClustDB

CLSK868994.

Family and domain databases

Gene3D

2.60.40.420. 1 hit.

InterPro

IPR014068. Azurin_proteobac.
IPR000923. BlueCu_1.
IPR008972. Cupredoxin.
[Graphical view]

Pfam

PF00127. Copper-bind. 1 hit.
[Graphical view]

SUPFAM

SSF49503. Cupredoxin. 1 hit.

TIGRFAMs

TIGR02695. azurin. 1 hit.

PROSITE

PS00196. COPPER_BLUE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00282.

Entry information

Entry name

AZUR_PSEAE

Accession

Primary (citable) accession number: P00282

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 1, 1989
Last modified:	May 29, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents