AZUP_ACHCY
ID AZUP_ACHCY Reviewed; 152 AA.
AC P19567; Q43929;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Pseudoazurin;
DE AltName: Full=Blue copper protein;
DE Flags: Precursor;
GN Name=bcp;
OS Achromobacter cycloclastes.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=223;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21921 / JCM 20009 / IAM 1013 / KCTC 2947 / LMG 1127 / NBRC
RC 102459 / An-17;
RX PubMed=8605003; DOI=10.1006/bbrc.1996.0249;
RA Chen J.-Y., Chang W.-C., Chang T., Chang W.-C., Liu M.-Y., Payne W.J.,
RA le Gall J.;
RT "Cloning, characterization, and expression of the nitric oxide-generating
RT nitrite reductase and of the blue copper protein genes of Achromobacter
RT cycloclastes.";
RL Biochem. Biophys. Res. Commun. 219:423-428(1996).
RN [2]
RP PROTEIN SEQUENCE OF 29-152.
RC STRAIN=ATCC 21921 / JCM 20009 / IAM 1013 / KCTC 2947 / LMG 1127 / NBRC
RC 102459 / An-17;
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 [3]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).
RC STRAIN=ATCC 21921 / JCM 20009 / IAM 1013 / KCTC 2947 / LMG 1127 / NBRC
RC 102459 / An-17;
RX PubMed=8138527; DOI=10.1093/oxfordjournals.jbchem.a124251;
RA Inoue T., Nishio N., Kai Y., Harada S., Ohshiro Y., Suzuki S., Kohzuma T.,
RA Shidara S., Iwasaki H.;
RT "Crystallization and preliminary X-ray studies on pseudoazurin from
RT Achromobacter cycloclastes IAM1013.";
RL J. Biochem. 114:761-762(1993).
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.
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DR EMBL; Z48669; CAA88588.1; -; Genomic_DNA.
DR PIR; JC4649; JC4649.
DR PDB; 1BQK; X-ray; 1.35 A; A=29-152.
DR PDB; 1BQR; X-ray; 1.60 A; A=29-152.
DR PDB; 1ZIA; X-ray; 1.54 A; A=29-152.
DR PDB; 1ZIB; X-ray; 2.00 A; A=29-152.
DR PDB; 2JKW; X-ray; 1.60 A; A/B=29-152.
DR PDB; 2UX6; X-ray; 1.30 A; A=29-152.
DR PDB; 2UX7; X-ray; 1.30 A; A=29-152.
DR PDB; 2UXF; X-ray; 2.00 A; A=29-152.
DR PDB; 2UXG; X-ray; 1.99 A; A=29-152.
DR PDB; 4YL4; X-ray; 1.10 A; A=29-152.
DR PDB; 5WV4; X-ray; 1.80 A; A/B=29-152.
DR PDB; 5XMO; X-ray; 1.19 A; A=29-152.
DR PDB; 5Y23; X-ray; 1.40 A; A/B=29-152.
DR PDB; 5YSG; X-ray; 2.00 A; A/B/C/D=29-152.
DR PDB; 5YW3; X-ray; 1.19 A; A/B/C/D=29-152.
DR PDB; 5Z0X; X-ray; 1.46 A; A/B=29-152.
DR PDB; 5ZTD; X-ray; 1.05 A; A/B=29-152.
DR PDB; 6AKN; X-ray; 1.19 A; A/B=29-152.
DR PDB; 6IFP; X-ray; 1.00 A; A/C=29-152.
DR PDBsum; 1BQK; -.
DR PDBsum; 1BQR; -.
DR PDBsum; 1ZIA; -.
DR PDBsum; 1ZIB; -.
DR PDBsum; 2JKW; -.
DR PDBsum; 2UX6; -.
DR PDBsum; 2UX7; -.
DR PDBsum; 2UXF; -.
DR PDBsum; 2UXG; -.
DR PDBsum; 4YL4; -.
DR PDBsum; 5WV4; -.
DR PDBsum; 5XMO; -.
DR PDBsum; 5Y23; -.
DR PDBsum; 5YSG; -.
DR PDBsum; 5YW3; -.
DR PDBsum; 5Z0X; -.
DR PDBsum; 5ZTD; -.
DR PDBsum; 6AKN; -.
DR PDBsum; 6IFP; -.
DR AlphaFoldDB; P19567; -.
DR SMR; P19567; -.
DR EvolutionaryTrace; P19567; -.
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..28
FT /evidence="ECO:0000269|PubMed:3595868"
FT CHAIN 29..152
FT /note="Pseudoazurin"
FT /id="PRO_0000002851"
FT DOMAIN 33..121
FT /note="Plastocyanin-like"
FT BINDING 68
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 109
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 114
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT CONFLICT 119
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 30..39
FT /evidence="ECO:0007829|PDB:6IFP"
FT STRAND 42..53
FT /evidence="ECO:0007829|PDB:6IFP"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:6IFP"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5ZTD"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:6IFP"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:6IFP"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:6IFP"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:6IFP"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:6IFP"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:6IFP"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:6IFP"
SQ SEQUENCE 152 AA; 15760 MW; 732F736DE38506D1 CRC64;
MEKTMLNAIK SGFGIAIAAM LVAAPAAAAD FEVHMLNKGK DGAMVFEPAS LKVAPGDTVT
FIPTDKGHNV ETIKGMIPDG AEAFKSKINE NYKVTFTAPG VYGVKCTPHY GMGMVGVVQV
GDAPANLEAV KGAKNPKKAQ ERLDAALAAL GN
