ID   AZUP_RHILV              Reviewed;         152 AA.
AC   Q52825;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Putative pseudoazurin;
DE   AltName: Full=Blue copper protein;
DE   Flags: Precursor;
GN   Name=azu;
OS   Rhizobium leguminosarum bv. viciae.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VF39;
RX   PubMed=8858582; DOI=10.1046/j.1365-2958.1996.6321348.x;
RA   Patschkowski T., Schlueter A., Priefer U.;
RT   "Rhizobium leguminosarum bv. viciae contains a second fnr/fixK-like gene
RT   and an unusual fixL homologue.";
RL   Mol. Microbiol. 21:267-280(1996).
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. {ECO:0000250}.
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   -!- MISCELLANEOUS: In R.leguminosarum (biovar viciae) pseudoazurin is
CC       dispensable for nitrogen fixation.
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DR   EMBL; Z70305; CAA94320.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q52825; -.
DR   SMR; Q52825; -.
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; 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.
PE   3: Inferred from homology;
KW   Copper; Electron transport; Metal-binding; Periplasm; Signal; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..152
FT                   /note="Putative pseudoazurin"
FT                   /id="PRO_0000002852"
FT   DOMAIN          28..116
FT                   /note="Plastocyanin-like"
FT   BINDING         63
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   152 AA;  16283 MW;  C561FF519F1ADD20 CRC64;
     MPLKFGLIVA TAALIASAAS LMAADHQVQM LNKGTDGAMV FEPGFLKIAP GDTVTFIPTD
     KSHNVETFKG LIPDGVPDFK SKPNEQYQVK FDIPGAYVLK CTPHVGMGMV ALIQVGDNPA
     NLEPIKIAKV PNMVRKRLDA DLAQITPAQI TQ