ID   AZUR1_METJ              Reviewed;         149 AA.
AC   P12334;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Azurin iso-1;
DE   Flags: Precursor;
OS   Methylomonas sp. (strain J).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=32038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9648216; DOI=10.1271/bbb.62.870;
RA   Taguchi K., Kudo T., Tobari J.;
RT   "Cloning and characterization of the azurin iso-1 gene, concerned with the
RT   electron transport chain involved in methylamine/methanol oxidation in the
RT   obligate methylotroph Methylomonas sp. strain J.";
RL   Biosci. Biotechnol. Biochem. 62:870-874(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-149.
RX   PubMed=2505762; DOI=10.1042/bj2610495;
RA   Ambler R.P., Tobari J.;
RT   "Two distinct azurins function in the electron-transport chain of the
RT   obligate methylotroph Methylomonas J.";
RL   Biochem. J. 261:495-499(1989).
CC   -!- FUNCTION: This methylothroph organism uses azurin in the electron
CC       transport chain involved in methylamine/methanol oxidation.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- INDUCTION: Produced during both methanol and methylamine growth. The
CC       expression of the azurin iso-1 gene is affected by copper ions.
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DR   PIR; JW0081; JW0081.
DR   AlphaFoldDB; P12334; -.
DR   SMR; P12334; -.
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   Copper; Direct protein sequencing; Disulfide bond; Electron transport;
KW   Metal-binding; Periplasm; Signal; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:2505762"
FT   CHAIN           22..149
FT                   /note="Azurin iso-1"
FT                   /id="PRO_0000002857"
FT   DOMAIN          22..149
FT                   /note="Plastocyanin-like"
FT   BINDING         67
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   DISULFID        24..47
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   149 AA;  15644 MW;  93344D8D49E2FDAF CRC64;
     MKSSKIVAIL LASLFSGSVL AAGCSVDVEA NDAMQYNTKN IDVEKSCKEF TVNLKHTGSL
     PKNVMGHNLV ITKTADFKAV MNDGVAAGEA GNFVKAGDAR VVAHTKLVGG GEKDSVKVDV
     SKLAAGEKYT FFCSFPGHAT MMRGTVTVK