ID   AZUP_PARDE              Reviewed;         123 AA.
AC   P80649;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Pseudoazurin;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 19367 / NBRC 13301 / NCIMB 8944 / NRRL B-3785;
RX   PubMed=9032456; DOI=10.1042/bj3210699;
RA   Leung Y.-C., Chan C., Reader J.S., Willis A.C., van Spanning R.J.M.,
RA   Ferguson S.J., Radford S.E.;
RT   "The pseudoazurin gene from Thiosphaera pantotropha: analysis of upstream
RT   putative regulatory sequences and overexpression in Escherichia coli.";
RL   Biochem. J. 321:699-705(1997).
CC   -!- FUNCTION: This soluble electron transfer copper protein is required for
CC       the inactivation of copper-containing nitrite reductase in the presence
CC       of oxygen.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC       Note=Binds 1 copper ion per subunit.;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P80649; -.
DR   SMR; P80649; -.
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; cd04218; Pseudoazurin; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR002386; Amicyanin/Pseudoazurin.
DR   InterPro; IPR000923; BlueCu_1.
DR   InterPro; IPR028871; BlueCu_1_BS.
DR   InterPro; IPR001235; Copper_blue_Plastocyanin.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR012745; Pseudoazurin.
DR   Pfam; PF00127; Copper-bind; 1.
DR   PRINTS; PR00155; AMICYANIN.
DR   PRINTS; PR00156; COPPERBLUE.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   TIGRFAMs; TIGR02375; pseudoazurin; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Electron transport; Metal-binding;
KW   Periplasm; Transport.
FT   CHAIN           1..123
FT                   /note="Pseudoazurin"
FT                   /id="PRO_0000085540"
FT   DOMAIN          5..93
FT                   /note="Plastocyanin-like"
FT   REGION          103..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   123 AA;  13337 MW;  983800FB8B5589E2 CRC64;
     ATHEVHMLNK GESGAMVFEP AFIRAEPGDV INFIPTDKSH NVEAIKEILP EGVETFKSKI
     NEAYALTVTE PGLYGVKCTP HFGMGMVGLV QVGDAPENLD AAQTAKMPKK ARERMDAELA
     QVN