AZUR_ACHDE
ID AZUR_ACHDE Reviewed; 149 AA.
AC P00280;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Azurin;
DE Flags: Precursor;
GN Name=azu;
OS Achromobacter denitrificans (Alcaligenes denitrificans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=32002;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2116366; DOI=10.1016/0378-1119(90)90434-s;
RA Hoitink C.W.G., Woudt L.P., Turenhout J.C.M., van de Kamp M., Canters G.W.;
RT "Isolation and sequencing of the Alcaligenes denitrificans azurin-encoding
RT gene: comparison with the genes encoding blue copper proteins from
RT Pseudomonas aeruginosa and Alcaligenes faecalis.";
RL Gene 90:15-20(1990).
RN [2]
RP PROTEIN SEQUENCE OF 21-149.
RC STRAIN=ATCC 15173 / DSM 30026 / JCM 5490 / NBRC 15125 / NCIMB 11961 / NCTC
RC 8582 / 55B;
RA Ambler R.P.;
RL Submitted (DEC-1974) to the PIR data bank.
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=6842609; DOI=10.1016/s0022-2836(83)80216-2;
RA Norris G.E., Anderson B.F., Baker E.N.;
RT "Structure of azurin from Alcaligenes denitrificans at 2.5-A resolution.";
RL J. Mol. Biol. 165:501-521(1983).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=3210236; DOI=10.1016/0022-2836(88)90129-5;
RA Baker E.N.;
RT "Structure of azurin from Alcaligenes denitrificans refinement at 1.8-A
RT resolution and comparison of the two crystallographically independent
RT molecules.";
RL J. Mol. Biol. 203:1071-1095(1988).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF GLN-141.
RX PubMed=8383207; DOI=10.1006/jmbi.1993.1101;
RA Romero A., Hoitink C.W., Nar H., Huber R., Messerschmidt A., Canters G.W.;
RT "X-ray analysis and spectroscopic characterization of M121Q azurin. A
RT copper site model for stellacyanin.";
RL J. Mol. Biol. 229:1007-1021(1993).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=8639662; DOI=10.1021/bi951748a;
RA Kroes S., Wamerdam G.C.M., Canters G.W.;
RT "Paramagnetic cobalt and nickel derivatives of Alcaligenes denitrificans
RT azurin and its M121Q mutant. A 1H NMR study.";
RL Biochemistry 35:1810-1819(1996).
CC -!- FUNCTION: Transfers electrons from cytochrome c551 to cytochrome
CC oxidase.
CC -!- SUBCELLULAR LOCATION: Periplasm.
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DR EMBL; M30388; AAA21954.1; -; Genomic_DNA.
DR PIR; JQ0643; AZALCD.
DR RefSeq; WP_062681289.1; NZ_UFRY01000001.1.
DR PDB; 1A4A; X-ray; 1.89 A; A/B=21-149.
DR PDB; 1A4B; X-ray; 1.91 A; A/B=21-149.
DR PDB; 1A4C; X-ray; 2.45 A; A/B/C/D=21-149.
DR PDB; 1AIZ; X-ray; 1.80 A; A/B=21-149.
DR PDB; 1AZB; X-ray; 2.20 A; A/B=21-149.
DR PDB; 1AZC; X-ray; 1.80 A; A/B=21-149.
DR PDB; 1URI; X-ray; 1.94 A; A/B=21-149.
DR PDB; 2AZA; X-ray; 1.80 A; A/B=21-149.
DR PDBsum; 1A4A; -.
DR PDBsum; 1A4B; -.
DR PDBsum; 1A4C; -.
DR PDBsum; 1AIZ; -.
DR PDBsum; 1AZB; -.
DR PDBsum; 1AZC; -.
DR PDBsum; 1URI; -.
DR PDBsum; 2AZA; -.
DR AlphaFoldDB; P00280; -.
DR SMR; P00280; -.
DR STRING; 32002.BVK87_22540; -.
DR GeneID; 56279836; -.
DR EvolutionaryTrace; P00280; -.
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; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 21..149
FT /note="Azurin"
FT /id="PRO_0000002858"
FT DOMAIN 21..149
FT /note="Plastocyanin-like"
FT BINDING 66
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:3210236"
FT BINDING 132
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:3210236"
FT BINDING 137
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:3210236"
FT BINDING 141
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:3210236"
FT DISULFID 23..46
FT CONFLICT 77
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1AIZ"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1A4A"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1AIZ"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:1AIZ"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1A4C"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1AIZ"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1AIZ"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:1AIZ"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:1AIZ"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1AIZ"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1AIZ"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:1AIZ"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1AIZ"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1AIZ"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1AIZ"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1AIZ"
SQ SEQUENCE 149 AA; 15924 MW; 849F182DD6B1BE3B CRC64;
MLAKATLAIV LSAASLPVLA AQCEATIESN DAMQYNLKEM VVDKSCKQFT VHLKHVGKMA
KVAMGHNWVL TKEADKQGVA TDGMNAGLAQ DYVKAGDTRV IAHTKVIGGG ESDSVTFDVS
KLTPGEAYAY FCSFPGHWAM MKGTLKLSN
