AMCY_PARVE
ID AMCY_PARVE Reviewed; 132 AA.
AC P22365;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Amicyanin;
DE Flags: Precursor;
GN Name=mauC; Synonyms=ami;
OS Paracoccus versutus (Thiobacillus versutus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=34007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1765062; DOI=10.1111/j.1432-1033.1991.tb16462.x;
RA Ubbink M., van Kleef M.A., Kleinjan D.J., Hoitink C.W., Huitema F.,
RA Beintema J.J., Duine J.A., Canters G.W.;
RT "Cloning, sequencing and expression studies of the genes encoding amicyanin
RT and the beta-subunit of methylamine dehydrogenase from Thiobacillus
RT versutus.";
RL Eur. J. Biochem. 202:1003-1012(1991).
RN [2]
RP PROTEIN SEQUENCE OF 27-132, AND PYROGLUTAMATE FORMATION AT GLN-27.
RX PubMed=2002033; DOI=10.1016/s0021-9258(19)67729-x;
RA van Beeumen J., van Bun S., Canters G.W., Lommen A., Chothia C.;
RT "The structural homology of amicyanin from Thiobacillus versutus to plant
RT plastocyanins.";
RL J. Biol. Chem. 266:4869-4877(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RX PubMed=8120896; DOI=10.1016/0022-2836(94)90021-3;
RA Romero A., Nar H., Huber R., Messerchmidt A., Kalverda A.P., Canters G.W.,
RA Durley R., Mathews F.S.;
RT "Crystal structure analysis and refinement at 2.15-A resolution of
RT amicyanin, a type I blue copper protein, from Thiobacillus versutus.";
RL J. Mol. Biol. 236:1196-1211(1994).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=1935963; DOI=10.1111/j.1432-1033.1991.tb16330.x;
RA Lommen A., Wijmenga S., Jilbers C.W., Canters G.W.;
RT "Assignment of the 600-MHz 1H-NMR spectrum of amicyanin from Thiobacillus
RT versutus by two-dimensional NMR methods provides information on secondary
RT structure.";
RL Eur. J. Biochem. 201:695-702(1991).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=8035459; DOI=10.1006/jmbi.1994.1450;
RA Kalverda A.P., Wymenga S.S., Lommen A., van de Ven F.J.M., Hilbers C.W.,
RA Canters G.W.;
RT "Solution structure of the type 1 blue copper protein amicyanin from
RT Thiobacillus versutus.";
RL J. Mol. Biol. 240:358-371(1994).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=9116004; DOI=10.1021/bi961960u;
RA Dennison C., Berg A., Canters G.W.;
RT "A 1H NMR study of the paramagnetic active site of the CuA variant of
RT amicyanin.";
RL Biochemistry 36:3262-3269(1997).
CC -!- FUNCTION: Primary acceptor of electrons from methylamine dehydrogenase.
CC Passes those electrons on either a soluble cytochrome c or to
CC pseudoazurin.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds 1 copper ion per subunit.;
CC -!- PATHWAY: One-carbon metabolism; methylamine degradation.
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; M58001; AAA50571.1; -; Genomic_DNA.
DR PIR; S19732; A23706.
DR RefSeq; WP_036750422.1; NZ_QUMX01000042.1.
DR PDB; 1ID2; X-ray; 2.15 A; A/B/C=27-132.
DR PDB; 3C75; X-ray; 2.50 A; A/B=1-132.
DR PDBsum; 1ID2; -.
DR PDBsum; 3C75; -.
DR AlphaFoldDB; P22365; -.
DR BMRB; P22365; -.
DR SMR; P22365; -.
DR STRING; 34007.IT40_03115; -.
DR eggNOG; COG3794; Bacteria.
DR OrthoDB; 1654242at2; -.
DR UniPathway; UPA00895; -.
DR EvolutionaryTrace; P22365; -.
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; cd13921; Amicyanin; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR035668; Amicyanin.
DR InterPro; IPR002386; Amicyanin/Pseudoazurin.
DR InterPro; IPR013475; Amicyanin_Para/Methyl.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR001235; Copper_blue_Plastocyanin.
DR InterPro; IPR008972; Cupredoxin.
DR Pfam; PF00127; Copper-bind; 1.
DR PRINTS; PR00155; AMICYANIN.
DR PRINTS; PR00156; COPPERBLUE.
DR SUPFAM; SSF49503; SSF49503; 1.
DR TIGRFAMs; TIGR02657; amicyanin; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Electron transport;
KW Metal-binding; Periplasm; Pyrrolidone carboxylic acid; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:2002033"
FT CHAIN 27..132
FT /note="Amicyanin"
FT /id="PRO_0000002845"
FT DOMAIN 27..132
FT /note="Plastocyanin-like"
FT BINDING 80
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 119
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 122
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 125
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT MOD_RES 27
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2002033"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1ID2"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1ID2"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1ID2"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:1ID2"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1ID2"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1ID2"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:1ID2"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1ID2"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1ID2"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:1ID2"
SQ SEQUENCE 132 AA; 14259 MW; 2E64C930BD18C41D CRC64;
MISAKTLRPA IAAIALFAIG ATGAWAQDKI TVTSEKPVAA ADVPADAVVV GIEKMKYLTP
EVTIKAGETV YWVNGEVMPH NVAFKKGIVG EDAFRGEMMT KDQAYAITFN EAGSYDYFCT
PHPFMRGKVI VE
