ID   AZUR2_ALCXX             Reviewed;         129 AA.
AC   P56275;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Azurin-2;
DE   AltName: Full=AZN-2;
DE   AltName: Full=Azurin-II;
OS   Alcaligenes xylosoxydans xylosoxydans (Achromobacter xylosoxidans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=85698;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=LMG 1865 / CCUG 61957 / NCIMB 11015 / Iwasaki;
RX   PubMed=7640272; DOI=10.1021/bi00032a011;
RA   Dodd F.E., Hasnain S.S., Hunter W.N., Abraham Z.H., Debenham M.,
RA   Kanzler H., Eldridge M., Eady R.R., Ambler R.P., Smith B.E.;
RT   "Evidence for two distinct azurins in Alcaligenes xylosoxidans (NCIMB
RT   11015): potential electron donors to nitrite reductase.";
RL   Biochemistry 34:10180-10186(1995).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=15299774; DOI=10.1107/s0907444995007554;
RA   Dodd F.E., Hasnain S.S., Eady R.R., Smith B.E.;
RT   "Structure of a new azurin from the denitrifying bacterium Alcaligenes
RT   xylosoxidans at high resolution.";
RL   Acta Crystallogr. D 51:1052-1064(1995).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RX   PubMed=10818345; DOI=10.1107/s0907444900003309;
RA   Dodd F.E., Abraham Z.H., Eady R.R., Hasnain S.S.;
RT   "Structures of oxidized and reduced azurin II from Alcaligenes xylosoxidans
RT   at 1.75-A resolution.";
RL   Acta Crystallogr. D 56:690-696(2000).
CC   -!- FUNCTION: Transfers electrons from cytochrome c551 to cytochrome
CC       oxidase.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
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DR   PIR; A58648; A58648.
DR   PDB; 1DYZ; X-ray; 1.75 A; A=1-129.
DR   PDB; 1DZ0; X-ray; 1.75 A; A=1-129.
DR   PDB; 2CCW; X-ray; 1.13 A; A=1-129.
DR   PDBsum; 1DYZ; -.
DR   PDBsum; 1DZ0; -.
DR   PDBsum; 2CCW; -.
DR   AlphaFoldDB; P56275; -.
DR   SMR; P56275; -.
DR   STRING; 1216976.AX27061_4415; -.
DR   eggNOG; COG3241; Bacteria.
DR   EvolutionaryTrace; P56275; -.
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; cd13922; Azurin; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR014068; Azurin.
DR   InterPro; IPR000923; BlueCu_1.
DR   InterPro; IPR028871; BlueCu_1_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   Pfam; PF00127; Copper-bind; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   TIGRFAMs; TIGR02695; azurin; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Metal-binding; Periplasm; Transport.
FT   CHAIN           1..129
FT                   /note="Azurin-2"
FT                   /id="PRO_0000085545"
FT   DOMAIN          1..129
FT                   /note="Plastocyanin-like"
FT   BINDING         46
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:15299774"
FT   BINDING         112
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:15299774"
FT   BINDING         117
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:15299774"
FT   BINDING         121
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:15299774"
FT   DISULFID        3..26
FT   STRAND          2..9
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   STRAND          27..35
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   HELIX           41..44
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   HELIX           56..66
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   HELIX           68..70
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:2CCW"
FT   STRAND          121..127
FT                   /evidence="ECO:0007829|PDB:2CCW"
SQ   SEQUENCE   129 AA;  13775 MW;  53E01A617CD725FC CRC64;
     AQCEATVESN DAMQYNVKEI VVDKSCKQFT MHLKHVGKMA KVAMGHNLVL TKDADKQAVA
     TDGMGAGLAQ DYVKAGDTRV IAHTKVIGGG ESDSVTFDVS KIAAGENYAY FCSFPGHWAM
     MKGTLKLGS