ID   AMCY_METEA              Reviewed;         119 AA.
AC   P04172; C5ATK8;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Amicyanin-alpha;
DE   Flags: Precursor;
GN   Name=mauC; OrderedLocusNames=MexAM1_META1p2774;
OS   Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS   9133 / AM1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=272630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1653226; DOI=10.1128/jb.173.18.5901-5908.1991;
RA   Chistoserdov A.Y., Tsygankov Y.D., Lidstrom M.E.;
RT   "Genetic organization of methylamine utilization genes from
RT   Methylobacterium extorquens AM1.";
RL   J. Bacteriol. 173:5901-5908(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8021187; DOI=10.1128/jb.176.13.4052-4065.1994;
RA   Chistoserdov A.Y., Chistoserdova L.V., McIntire W.S., Lidstrom M.E.;
RT   "Genetic organization of the mau gene cluster in Methylobacterium
RT   extorquens AM1: complete nucleotide sequence and generation and
RT   characteristics of mau mutants.";
RL   J. Bacteriol. 176:4052-4065(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
RN   [4]
RP   PROTEIN SEQUENCE OF 21-119.
RX   PubMed=4091802; DOI=10.1042/bj2320451;
RA   Ambler R.P., Tobari J.;
RT   "The primary structures of Pseudomonas AM1 amicyanin and pseudoazurin. Two
RT   new sequence classes of blue copper proteins.";
RL   Biochem. J. 232:451-457(1985).
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.
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DR   EMBL; M57963; AAA68895.1; -; Genomic_DNA.
DR   EMBL; L26406; AAB46937.1; -; Genomic_DNA.
DR   EMBL; CP001510; ACS40532.1; -; Genomic_DNA.
DR   PIR; A56621; CUPSAM.
DR   RefSeq; WP_012753047.1; NC_012808.1.
DR   AlphaFoldDB; P04172; -.
DR   SMR; P04172; -.
DR   STRING; 272630.MexAM1_META1p2774; -.
DR   EnsemblBacteria; ACS40532; ACS40532; MexAM1_META1p2774.
DR   KEGG; mea:Mex_1p2774; -.
DR   eggNOG; COG3794; Bacteria.
DR   HOGENOM; CLU_084115_4_0_5; -.
DR   OMA; CTPHPFM; -.
DR   OrthoDB; 1654242at2; -.
DR   UniPathway; UPA00895; -.
DR   Proteomes; UP000009081; Chromosome.
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; IPR008972; Cupredoxin.
DR   Pfam; PF00127; Copper-bind; 1.
DR   PRINTS; PR00155; AMICYANIN.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   TIGRFAMs; TIGR02657; amicyanin; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Electron transport; Metal-binding;
KW   Periplasm; Signal; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:4091802"
FT   CHAIN           21..119
FT                   /note="Amicyanin-alpha"
FT                   /evidence="ECO:0000269|PubMed:4091802"
FT                   /id="PRO_0000002843"
FT   DOMAIN          21..119
FT                   /note="Plastocyanin-like"
FT   BINDING         67
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   119 AA;  12609 MW;  732FDECA8239D857 CRC64;
     MRALAFAAAL AAFSATAALA AGALEAVQEA PAGSTEVKIA KMKFQTPEVR IKAGSAVTWT
     NTEALPHNVH FKSGPGVEKD VEGPMLRSNQ TYSVKFNAPG TYDYICTPHP FMKGKVVVE