AZUR1_ALCXX
ID AZUR1_ALCXX Reviewed; 129 AA.
AC P56547;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Azurin-1;
DE AltName: Full=AZN-1;
DE AltName: Full=Azurin-I;
OS Alcaligenes xylosoxydans xylosoxydans (Achromobacter xylosoxidans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=85698;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RC STRAIN=LMG 1865 / CCUG 61957 / NCIMB 11015 / Iwasaki;
RX PubMed=9761902; DOI=10.1107/s0907444997010974;
RA Li C., Inoue T., Gotowda M., Suzuki S., Yamaguchi K., Kataoka K., Kai Y.;
RT "Structure of azurin I from the denitrifying bacterium Alcaligenes
RT xylosoxidans NCIMB 11015 at 2.45-A resolution.";
RL Acta Crystallogr. D 54:347-354(1998).
CC -!- FUNCTION: Transfers electrons from cytochrome c551 to cytochrome
CC oxidase.
CC -!- SUBCELLULAR LOCATION: Periplasm.
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DR PDB; 1RKR; X-ray; 2.45 A; A/B/C/D=1-129.
DR PDB; 6L1V; X-ray; 2.25 A; A/C/E/G=1-129.
DR PDBsum; 1RKR; -.
DR PDBsum; 6L1V; -.
DR AlphaFoldDB; P56547; -.
DR SMR; P56547; -.
DR STRING; 1216976.AX27061_5009; -.
DR eggNOG; COG3241; Bacteria.
DR EvolutionaryTrace; P56547; -.
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; Disulfide bond; Electron transport; Metal-binding;
KW Periplasm; Transport.
FT CHAIN 1..129
FT /note="Azurin-1"
FT /id="PRO_0000085544"
FT DOMAIN 1..129
FT /note="Plastocyanin-like"
FT BINDING 46
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 112
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 117
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT DISULFID 3..26
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:6L1V"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:6L1V"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:6L1V"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:6L1V"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:6L1V"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6L1V"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6L1V"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:6L1V"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6L1V"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6L1V"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:6L1V"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6L1V"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6L1V"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6L1V"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:6L1V"
SQ SEQUENCE 129 AA; 13886 MW; F2BA0340D0519F53 CRC64;
AECSVDIAGN DGMQFDKKEI TVSKSCKQFT VNLKHPGKLA KNVMGHNWVL TKQADMQGAV
NDGMAAGLDN NYVKKDDARV IAHTKVIGGG ETDSVTFDVS KLAAGEDYAY FCSFPGHFAL
MKGVLKLVD
