AZUP_ALCFA
ID AZUP_ALCFA Reviewed; 146 AA.
AC P04377;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Pseudoazurin;
DE AltName: Full=Blue copper protein;
DE AltName: Full=Cupredoxin;
DE Flags: Precursor;
OS Alcaligenes faecalis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Alcaligenes.
OX NCBI_TaxID=511;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S-6;
RX PubMed=2824441; DOI=10.1128/jb.169.12.5648-5652.1987;
RA Yamamoto K., Uozumi T., Beppu T.;
RT "The blue copper protein gene of Alcaligenes faecalis S-6 directs secretion
RT of blue copper protein from Escherichia coli cells.";
RL J. Bacteriol. 169:5648-5652(1987).
RN [2]
RP PROTEIN SEQUENCE OF 24-146.
RC STRAIN=S-6;
RX PubMed=3512305; DOI=10.1016/0014-5793(86)80346-5;
RA Hormel S., Adman E.T., Walsh K.A., Beppu T., Titani K.;
RT "The amino acid sequence of the blue copper protein of Alcaligenes
RT faecalis.";
RL FEBS Lett. 197:301-304(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC STRAIN=S-6;
RX PubMed=3595868; DOI=10.1016/0014-5793(87)81048-7;
RA Petratos K., Banner D.W., Beppu T., Wilson K.S., Tsernoglou D.;
RT "The crystal structure of pseudoazurin from Alcaligenes faecalis S-6
RT determined at 2.9-A resolution.";
RL FEBS Lett. 218:209-214(1987).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC STRAIN=S-6;
RX PubMed=2909547; DOI=10.1016/s0021-9258(17)31227-9;
RA Adman E.T., Turley S., Bramson R., Petratos K., Banner D., Tsernoglou D.,
RA Beppu T., Watanabe H.;
RT "A 2.0-A structure of the blue copper protein (cupredoxin) from Alcaligenes
RT faecalis S-6.";
RL J. Biol. Chem. 264:87-99(1989).
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. Serves as a direct electron donor to the nitrite reductase.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds 1 copper ion per subunit.;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: Under anaerobic growth conditions and by nitrite.
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DR EMBL; M18267; AAA21955.1; -; Genomic_DNA.
DR PIR; A28385; CUALBF.
DR PDB; 1PAZ; X-ray; 1.55 A; A=24-146.
DR PDB; 1PY0; X-ray; 2.00 A; A=24-146.
DR PDB; 1PZA; X-ray; 1.80 A; A=24-146.
DR PDB; 1PZB; X-ray; 1.80 A; A=24-146.
DR PDB; 1PZC; X-ray; 1.85 A; A=24-146.
DR PDB; 2P80; NMR; -; D=24-146.
DR PDB; 3NYK; X-ray; 1.86 A; A=24-146.
DR PDB; 3PAZ; X-ray; 1.73 A; A=24-146.
DR PDB; 4PAZ; X-ray; 1.76 A; A=24-146.
DR PDB; 4RH4; X-ray; 1.60 A; A=24-146.
DR PDB; 5PAZ; X-ray; 1.76 A; A=24-146.
DR PDB; 5X31; X-ray; 2.60 A; A/B=24-146.
DR PDB; 6PAZ; X-ray; 1.91 A; A=24-146.
DR PDB; 7PAZ; X-ray; 2.00 A; A=24-146.
DR PDB; 8PAZ; X-ray; 1.60 A; A=24-146.
DR PDBsum; 1PAZ; -.
DR PDBsum; 1PY0; -.
DR PDBsum; 1PZA; -.
DR PDBsum; 1PZB; -.
DR PDBsum; 1PZC; -.
DR PDBsum; 2P80; -.
DR PDBsum; 3NYK; -.
DR PDBsum; 3PAZ; -.
DR PDBsum; 4PAZ; -.
DR PDBsum; 4RH4; -.
DR PDBsum; 5PAZ; -.
DR PDBsum; 5X31; -.
DR PDBsum; 6PAZ; -.
DR PDBsum; 7PAZ; -.
DR PDBsum; 8PAZ; -.
DR AlphaFoldDB; P04377; -.
DR BMRB; P04377; -.
DR SMR; P04377; -.
DR DrugBank; DB04229; 7,10,13-Tri(Carboxymethyl)-5,15-Dioxo-4,7,10,13,16-Pentaaza-1,19-Dithianonadecane.
DR EvolutionaryTrace; P04377; -.
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 3D-structure; Copper; Direct protein sequencing; Electron transport;
KW Metal-binding; Periplasm; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:3512305"
FT CHAIN 24..146
FT /note="Pseudoazurin"
FT /id="PRO_0000002849"
FT DOMAIN 28..116
FT /note="Plastocyanin-like"
FT BINDING 63
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:2909547"
FT BINDING 101
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:2909547"
FT BINDING 104
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:2909547"
FT BINDING 109
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:2909547"
FT STRAND 25..34
FT /evidence="ECO:0007829|PDB:1PAZ"
FT STRAND 37..48
FT /evidence="ECO:0007829|PDB:1PAZ"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:1PAZ"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1PAZ"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1PAZ"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1PAZ"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1PAZ"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:1PAZ"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:1PAZ"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:1PAZ"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:7PAZ"
SQ SEQUENCE 146 AA; 15647 MW; E4093B9A289F947F CRC64;
MRNIAIKFAA AGILAMLAAP ALAENIEVHM LNKGAEGAMV FEPAYIKANP GDTVTFIPVD
KGHNVESIKD MIPEGAEKFK SKINENYVLT VTQPGAYLVK CTPHYAMGMI ALIAVGDSPA
NLDQIVSAKK PKIVQERLEK VIASAK
