ID   AZUR5_PSEPU             Reviewed;         148 AA.
AC   Q9F646;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Azurin {ECO:0000312|EMBL:AAG27699.1};
DE   Flags: Precursor;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAG27699.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MASS SPECTROMETRY.
RC   STRAIN=HK5 {ECO:0000269|PubMed:11515547};
RX   PubMed=11515547; DOI=10.1271/bbb.65.1617;
RA   Toyama H., Aoki N., Matsushita K., Adachi O.;
RT   "Azurin involved in alcohol oxidation system in Pseudomonas putida HK5:
RT   expression analysis and gene cloning.";
RL   Biosci. Biotechnol. Biochem. 65:1617-1626(2001).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 21-39, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=HK5 {ECO:0000269|PubMed:10320337};
RX   PubMed=10320337; DOI=10.1021/bi990121f;
RA   Matsushita K., Yamashita T., Aoki N., Toyama H., Adachi O.;
RT   "Electron transfer from quinohemoprotein alcohol dehydrogenase to blue
RT   copper protein azurin in the alcohol oxidase respiratory chain of
RT   Pseudomonas putida HK5.";
RL   Biochemistry 38:6111-6118(1999).
CC   -!- FUNCTION: Transfers electrons from cytochrome c551 to cytochrome
CC       oxidase. {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:11515547}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=276 nm {ECO:0000269|PubMed:10320337};
CC         Note=Exhibits a broad peak at 623 nm. The above maxima are for the
CC         oxidized form. {ECO:0000269|PubMed:10320337};
CC       Redox potential:
CC         E(0) is +306 mV for copper at pH 7.0, +280 mV for copper at pH 8.0,
CC         +291 mV for ADH IIB-azurin complex, +286 mV at pH 8.0 and 0.3 M KCl
CC         and +298 mV for ADH IIB-azurin complex.
CC         {ECO:0000269|PubMed:10320337};
CC   -!- SUBUNIT: Monomer with an intramolecular disulfide bond but can also
CC       exist a dimer with an intermolecular disulfide bond.
CC       {ECO:0000269|PubMed:10320337}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P34097}.
CC   -!- MASS SPECTROMETRY: Mass=13914; Method=MALDI; Note=Mass determined
CC       without bound copper ion.; Evidence={ECO:0000269|PubMed:11515547};
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DR   EMBL; AF299296; AAG27699.1; -; Genomic_DNA.
DR   RefSeq; WP_043863517.1; NZ_RJUR01000015.1.
DR   AlphaFoldDB; Q9F646; -.
DR   SMR; Q9F646; -.
DR   SABIO-RK; Q9F646; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
DR   CDD; cd13922; Azurin; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR014068; Azurin.
DR   InterPro; IPR000923; BlueCu_1.
DR   InterPro; IPR008972; Cupredoxin.
DR   Pfam; PF00127; Copper-bind; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   TIGRFAMs; TIGR02695; azurin; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Disulfide bond; Electron transport;
KW   Metal-binding; Periplasm; Signal; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:10320337"
FT   CHAIN           21..148
FT                   /note="Azurin"
FT                   /evidence="ECO:0000312|EMBL:AAG27699.1"
FT                   /id="PRO_5000058632"
FT   DOMAIN          21..148
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000255"
FT   BINDING         66
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P34097"
FT   BINDING         132
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P34097"
FT   BINDING         137
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P34097"
FT   BINDING         141
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P34097"
FT   DISULFID        23..46
FT                   /evidence="ECO:0000250|UniProtKB:P34097"
SQ   SEQUENCE   148 AA;  15926 MW;  A8230D85300AEE1C CRC64;
     MFAKAVAVSL LTLASAQVFA ADCKVTVDST DQMSFNTKAI EIDKSCKTFT VELTHSGNLP
     KNVMGHNLVI SKEADMQPIA TDGLSAGIDK DYLKEGDDRV IAHTKVIGAG EKDSVTFDVS
     KLKADEKYGF FCSFPGHISM MKGTVTLK