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 04-NOV-2026, entry version 130. DE RecName: Full=Pseudoazurin; DE AltName: Full=Blue copper protein; DE AltName: Full=Cupredoxin; DE Flags: Precursor; OS Alcaligenes faecalis. OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; 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. 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. 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. 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 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; 8K9N; X-ray; 0.86 A; A=24-146. DR PDB; 8K9P; Other; 1.50 A; A=24-146. DR PDB; 8PAZ; X-ray; 1.60 A; A=24-146. DR AlphaFoldDB; P04377; -. DR BMRB; P04377; -. DR MDposit; 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; Cupredoxins - blue copper proteins; 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 NCBIfam; TIGR02375; pseudoazurin; 1. DR Pfam; PF00127; Copper-bind; 1. DR PRINTS; PR00155; AMICYANIN. DR PRINTS; PR00156; COPPERBLUE. DR SUPFAM; SSF49503; Cupredoxins; 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:8K9N" FT STRAND 37..48 FT /evidence="ECO:0007829|PDB:8K9N" FT STRAND 52..57 FT /evidence="ECO:0007829|PDB:8K9N" FT STRAND 59..62 FT /evidence="ECO:0007829|PDB:8K9N" FT STRAND 87..91 FT /evidence="ECO:0007829|PDB:8K9N" FT STRAND 93..100 FT /evidence="ECO:0007829|PDB:8K9N" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:8K9N" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:8K9N" FT STRAND 110..118 FT /evidence="ECO:0007829|PDB:8K9N" FT HELIX 122..127 FT /evidence="ECO:0007829|PDB:8K9N" FT HELIX 132..145 FT /evidence="ECO:0007829|PDB:8K9N" SQ SEQUENCE 146 AA; 15647 MW; E4093B9A289F947F CRC64; MRNIAIKFAA AGILAMLAAP ALAENIEVHM LNKGAEGAMV FEPAYIKANP GDTVTFIPVD KGHNVESIKD MIPEGAEKFK SKINENYVLT VTQPGAYLVK CTPHYAMGMI ALIAVGDSPA NLDQIVSAKK PKIVQERLEK VIASAK //