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 10-JUN-2026, entry version 130. DE RecName: Full=Azurin; DE Flags: Precursor; GN Name=azu; OS Achromobacter denitrificans (Alcaligenes denitrificans). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; 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 / RC NCTC 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M30388; AAA21954.1; -; Genomic_DNA. DR PIR; JQ0643; AZALCD. DR RefSeq; WP_062681289.1; NZ_BLWG01000771.1. 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 AlphaFoldDB; P00280; -. DR SMR; P00280; -. DR STRING; 32002.BVK87_22540; -. DR PaxDb; 32002-BVK87_22540; -. DR GeneID; 92845278; -. DR OrthoDB; 9814063at2; -. 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 FunFam; 2.60.40.420:FF:000040; Azurin; 1. DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1. DR InterPro; IPR014068; Azurin. DR InterPro; IPR000923; BlueCu_1. DR InterPro; IPR028871; BlueCu_1_BS. DR InterPro; IPR050845; Cu-binding_ET. DR InterPro; IPR008972; Cupredoxin. DR NCBIfam; TIGR02695; azurin; 1. DR PANTHER; PTHR38439; AURACYANIN-B; 1. DR PANTHER; PTHR38439:SF2; OUTER MEMBRANE PROTEIN H.8; 1. DR Pfam; PF00127; Copper-bind; 1. DR SUPFAM; SSF49503; Cupredoxins; 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 TURN 138..140 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 //