AZUR2_METJ
ID AZUR2_METJ Reviewed; 129 AA.
AC P12335;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Azurin iso-2;
OS Methylomonas sp. (strain J).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=32038;
RN [1]
RP PROTEIN SEQUENCE.
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=10631606; DOI=10.1007/pl00010653;
RA Suzuki S., Nakamura N., Yamaguchi K., Kataoka K., Inoue T., Nishio N.,
RA Kai Y., Tobari J.;
RT "Spectroscopic and electrochemical properties of two azurins (Az-iso1 and
RT Az-iso2) from the obligate methylotroph Methylomonas sp. strain J and the
RT structure of novel Az-iso2.";
RL J. Biol. Inorg. Chem. 4:749-758(1999).
CC -!- FUNCTION: This methylothroph organism uses azurin in the oxidation of
CC methylamine. Iso-2 is probably the acceptor of electrons from
CC methylamine dehydrogenase.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: Produced during growth on methylamine.
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DR PIR; S05247; S05247.
DR PDB; 1CUO; X-ray; 1.60 A; A=1-129.
DR PDB; 1UAT; X-ray; 1.90 A; A=1-129.
DR PDBsum; 1CUO; -.
DR PDBsum; 1UAT; -.
DR AlphaFoldDB; P12335; -.
DR SMR; P12335; -.
DR EvolutionaryTrace; P12335; -.
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 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..129
FT /note="Azurin iso-2"
FT /id="PRO_0000085541"
FT DOMAIN 1..129
FT /note="Plastocyanin-like"
FT BINDING 46
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 112
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 117
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT DISULFID 3..26
FT /evidence="ECO:0000250"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1CUO"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1CUO"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1CUO"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:1CUO"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1CUO"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1CUO"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1CUO"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1CUO"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:1CUO"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1CUO"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1CUO"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1CUO"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1CUO"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1CUO"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1CUO"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1CUO"
SQ SEQUENCE 129 AA; 13805 MW; 872C6E5B09078BED CRC64;
ASCETTVTSG DTMTYSTRSI SVPASCAEFT VNFEHKGHMP KTGMGHNWVL AKSADVGDVA
KEGAHAGADN NFVTPGDKRV IAFTPIIGGG EKTSVKFKVS ALSKDEAYTY FCSYPGHFSM
MRGTLKLEE