ID   AZUR_PSEPU              Reviewed;         128 AA.
AC   P34097;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Azurin;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=NCIMB 9869;
RX   PubMed=8489263; DOI=10.1006/abbi.1993.1250;
RA   Barber M.J., Trimboli A., McIntire W.S.;
RT   "The amino acid sequence of Pseudomonas putida azurin.";
RL   Arch. Biochem. Biophys. 303:22-26(1993).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS).
RC   STRAIN=NCIMB 9869;
RX   PubMed=9761890; DOI=10.1107/s0907444997011505;
RA   Chen Z.-W., Barber M.J., McIntire W.S., Mathews F.S.;
RT   "Crystallographic study of azurin from Pseudomonas putida.";
RL   Acta Crystallogr. D 54:253-268(1998).
CC   -!- FUNCTION: Transfers electrons from cytochrome c551 to cytochrome
CC       oxidase.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
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DR   PIR; S33271; A37338.
DR   PDB; 1NWO; X-ray; 1.92 A; A/B=1-128.
DR   PDB; 1NWP; X-ray; 1.60 A; A/B=1-128.
DR   PDBsum; 1NWO; -.
DR   PDBsum; 1NWP; -.
DR   AlphaFoldDB; P34097; -.
DR   SMR; P34097; -.
DR   EvolutionaryTrace; P34097; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   CDD; cd13922; Azurin; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR014068; Azurin.
DR   InterPro; IPR000923; BlueCu_1.
DR   InterPro; IPR028871; BlueCu_1_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   Pfam; PF00127; Copper-bind; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   TIGRFAMs; TIGR02695; azurin; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Metal-binding; Periplasm; Transport.
FT   CHAIN           1..128
FT                   /note="Azurin"
FT                   /id="PRO_0000085551"
FT   DOMAIN          1..128
FT                   /note="Plastocyanin-like"
FT   BINDING         46
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT   BINDING         112
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT   BINDING         117
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT   BINDING         121
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT   DISULFID        3..26
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   STRAND          18..23
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   STRAND          27..35
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   HELIX           41..44
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   HELIX           56..63
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   HELIX           68..70
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:1NWP"
FT   STRAND          121..128
FT                   /evidence="ECO:0007829|PDB:1NWP"
SQ   SEQUENCE   128 AA;  13719 MW;  1919ABE6FEECE018 CRC64;
     AECKVTVDST DQMSFNTKDI AIDKSCKTFT VELTHSGSLP KNVMGHNLVI SKEADMQPIA
     TDGLSAGIDK QYLKDGDARV IAHTKVIGAG EKDSVTFDVS KLAAGEKYGF FCSFPGHISM
     MKGTVTLK