ID   AZUR_PSEFA              Reviewed;         128 AA.
AC   P80546;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Azurin;
OS   Pseudomonas fluorescens biotype A.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=32035;
RN   [1]
RP   PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RC   STRAIN=ATCC 13525 / DSM 50090 / JCM 5963 / NBRC 14160 / NCIMB 9046 / NCTC
RC   10038 / VKM B-894;
RX   PubMed=15299879; DOI=10.1107/s0907444997001509;
RA   Lee X., Dahms T., Ton-That H., Zhu D.-W., Biesterfeldt J., Lanthier P.H.,
RA   Yaguchi M., Szabo A.G.;
RT   "Primary sequence and refined tertiary structure of Pseudomonas fluorescens
RT   holo azurin at 2.05 A.";
RL   Acta Crystallogr. D 53:493-506(1997).
CC   -!- FUNCTION: Transfers electrons from cytochrome c551 to cytochrome
CC       oxidase.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
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DR   PDB; 1JOI; X-ray; 2.05 A; A=1-128.
DR   PDBsum; 1JOI; -.
DR   AlphaFoldDB; P80546; -.
DR   SMR; P80546; -.
DR   PRIDE; P80546; -.
DR   EvolutionaryTrace; P80546; -.
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_0000085548"
FT   DOMAIN          1..128
FT                   /note="Plastocyanin-like"
FT   BINDING         46
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   DISULFID        3..26
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:1JOI"
FT   STRAND          18..23
FT                   /evidence="ECO:0007829|PDB:1JOI"
FT   STRAND          27..35
FT                   /evidence="ECO:0007829|PDB:1JOI"
FT   HELIX           41..44
FT                   /evidence="ECO:0007829|PDB:1JOI"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:1JOI"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:1JOI"
FT   HELIX           56..66
FT                   /evidence="ECO:0007829|PDB:1JOI"
FT   HELIX           68..70
FT                   /evidence="ECO:0007829|PDB:1JOI"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:1JOI"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:1JOI"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:1JOI"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:1JOI"
FT   STRAND          121..128
FT                   /evidence="ECO:0007829|PDB:1JOI"
SQ   SEQUENCE   128 AA;  13639 MW;  AA74F8E2410F467C CRC64;
     AECKVTVDST DQMSFNTKAI EIDKSCKTFT VELTHSGSLP KNVMGHNWVL SSAADMPGIA
     SDGMAAGIDK NYLKEGDIRV IAHTKIIGAG EKDSVTFDVS KLAAGTDYAF FCSFPGHISM
     MKGTVTVK