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Protein

Azurin

Gene

azu

Organism
Achromobacter denitrificans (Alcaligenes denitrificans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transfers electrons from cytochrome c551 to cytochrome oxidase.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi66 – 661Copper1 Publication
Metal bindingi132 – 1321Copper1 Publication
Metal bindingi137 – 1371Copper1 Publication
Metal bindingi141 – 1411Copper1 Publication

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:
Azurin
Gene namesi
Name:azu
OrganismiAchromobacter denitrificans (Alcaligenes denitrificans)
Taxonomic identifieri32002 [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 – 20201 PublicationAdd
BLAST
Chaini21 – 149129AzurinPRO_0000002858Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi23 ↔ 46

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
149
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 297Combined sources
Beta strandi31 – 333Combined sources
Beta strandi38 – 436Combined sources
Beta strandi47 – 559Combined sources
Beta strandi57 – 593Combined sources
Helixi61 – 644Combined sources
Beta strandi69 – 724Combined sources
Turni73 – 753Combined sources
Helixi76 – 849Combined sources
Helixi88 – 903Combined sources
Beta strandi100 – 1034Combined sources
Beta strandi112 – 1187Combined sources
Helixi119 – 1213Combined sources
Beta strandi127 – 1315Combined sources
Helixi137 – 1393Combined sources
Beta strandi141 – 1488Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00280.
SMRiP00280. Positions 21-149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00280.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 149129Plastocyanin-likeAdd
BLAST

Sequence similaritiesi

Contains 1 plastocyanin-like domain.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR014068. Azurin_proteobac.
IPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00127. Copper-bind. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
TIGRFAMsiTIGR02695. azurin. 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.

P00280-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAKATLAIV LSAASLPVLA AQCEATIESN DAMQYNLKEM VVDKSCKQFT
60 70 80 90 100
VHLKHVGKMA KVAMGHNWVL TKEADKQGVA TDGMNAGLAQ DYVKAGDTRV
110 120 130 140
IAHTKVIGGG ESDSVTFDVS KLTPGEAYAY FCSFPGHWAM MKGTLKLSN
Length:149
Mass (Da):15,924
Last modified:November 1, 1990 - v2
Checksum:i849F182DD6B1BE3B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771Q → E AA sequence (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30388 Genomic DNA. Translation: AAA21954.1.
PIRiJQ0643. AZALCD.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30388 Genomic DNA. Translation: AAA21954.1.
PIRiJQ0643. AZALCD.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00280.
SMRiP00280. Positions 21-149.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00280.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR014068. Azurin_proteobac.
IPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00127. Copper-bind. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
TIGRFAMsiTIGR02695. azurin. 1 hit.
PROSITEiPS00196. COPPER_BLUE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiAZUR_ACHDE
AccessioniPrimary (citable) accession number: P00280
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: October 14, 2015
This is version 99 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.