AZUR_ALCFA
ID AZUR_ALCFA Reviewed; 128 AA.
AC P00281;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Azurin;
OS Alcaligenes faecalis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Alcaligenes.
OX NCBI_TaxID=511;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 8750 / DSM 30030 / CCUG 1814 / LMG 1229 / NBRC 13111 / NCIMB
RC 8156 / NCTC 11953 / Conn 16;
RA Ambler R.P.;
RL (In) Preverio A., Pechere J.-F., Coletti-preverio M.-A. (eds.);
RL Developpements recents dans l'etude chimique de la structure des proteines,
RL pp.289-305, INSERM, Paris (1971).
RN [2]
RP FUNCTION.
RX PubMed=6274637; DOI=10.1111/j.1432-1033.1981.tb05709.x;
RA Rosen P., Segal M., Pecht I.;
RT "Electron transfer between azurin from Alcaligenes faecalis and cytochrome
RT c551 from Pseudomonas aeruginosa.";
RL Eur. J. Biochem. 120:339-344(1981).
RN [3]
RP COFACTOR.
RX PubMed=6960351; DOI=10.1073/pnas.79.22.6807;
RA Mitra S., Bersohn R.;
RT "Proton NMR of the histidines of azurin from Alcaligenes faecalis: linkage
RT of histidine-35 with redox kinetics.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:6807-6811(1982).
RN [4]
RP COFACTOR.
RX PubMed=6232270; DOI=10.1016/s0021-9258(17)42919-x;
RA Engeseth H.R., McMillin D.R., Otvos J.D.;
RT "Comparative Cd-113 nuclear magnetic resonance studies of Cd(II)-
RT substituted blue copper proteins.";
RL J. Biol. Chem. 259:4822-4826(1984).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH COPPER; AAUA AND
RP AAUB, FUNCTION, COFACTOR, SUBUNIT, AND DISULFIDE BONDS.
RC STRAIN=ATCC 49677 / NBRC 14479;
RX PubMed=17087503; DOI=10.1021/bi0612972;
RA Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D.,
RA Chistoserdov A.Y., Davidson V.L., Mathews F.S.;
RT "Crystal structure of an electron transfer complex between aromatic amine
RT dehydrogenase and azurin from Alcaligenes faecalis.";
RL Biochemistry 45:13500-13510(2006).
CC -!- FUNCTION: Transfers electrons from cytochrome c551 to cytochrome
CC oxidase. Transfers electrons from the tryptophan tryptophylquinone of
CC the aromatic amine dehydrogenase heterotetramer.
CC {ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:6274637}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:6232270,
CC ECO:0000269|PubMed:6960351};
CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:17087503,
CC ECO:0000269|PubMed:6232270, ECO:0000269|PubMed:6960351};
CC -!- SUBUNIT: Monomer. Interacts with the AAUA/AAUB heterotetramer complex.
CC {ECO:0000269|PubMed:17087503}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
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DR PIR; A00287; AZALCF.
DR PDB; 2H3X; X-ray; 2.50 A; C/F=1-128.
DR PDB; 2H47; X-ray; 2.60 A; C=1-128.
DR PDB; 2IAA; X-ray; 1.95 A; C=1-128.
DR PDBsum; 2H3X; -.
DR PDBsum; 2H47; -.
DR PDBsum; 2IAA; -.
DR AlphaFoldDB; P00281; -.
DR SMR; P00281; -.
DR STRING; 511.JT27_05730; -.
DR eggNOG; COG3241; Bacteria.
DR EvolutionaryTrace; P00281; -.
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..128
FT /note="Azurin"
FT /id="PRO_0000085542"
FT DOMAIN 1..128
FT /note="Plastocyanin-like"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:17087503"
FT BINDING 111
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:17087503"
FT BINDING 116
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:17087503"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:17087503"
FT DISULFID 2..25
FT /evidence="ECO:0000269|PubMed:17087503"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2IAA"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:2IAA"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:2IAA"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:2IAA"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:2IAA"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:2IAA"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2IAA"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:2IAA"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:2IAA"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2IAA"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:2IAA"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:2IAA"
SQ SEQUENCE 128 AA; 13693 MW; E523FBE3DC5D168C CRC64;
ACDVSIEGND SMQFNTKSIV VDKTCKEFTI NLKHTGKLPK AAMGHNVVVS KKSDESAVAT
DGMKAGLNND YVKAGDERVI AHTSVIGGGE TDSVTFDVSK LKEGEDYAFF CSFPGHWSIM
KGTIELGS
