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Database: UniProt
Entry: A0A0G3A7X1_9ACTN
LinkDB: A0A0G3A7X1_9ACTN
Original site: A0A0G3A7X1_9ACTN 
ID   A0A0G3A7X1_9ACTN        Unreviewed;       630 AA.
AC   A0A0G3A7X1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Phenoxazinone synthase {ECO:0000313|EMBL:AKJ09968.1};
GN   ORFNames=ABB07_08015 {ECO:0000313|EMBL:AKJ09968.1};
OS   Streptomyces incarnatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ09968.1, ECO:0000313|Proteomes:UP000035366};
RN   [1] {ECO:0000313|EMBL:AKJ09968.1, ECO:0000313|Proteomes:UP000035366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX   PubMed=26159526;
RA   Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA   Tamura T.;
RT   "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT   the Nucleoside Antibiotic Sinefungin.";
RL   Genome Announc. 3:e00715-e00715(2015).
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DR   EMBL; CP011497; AKJ09968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G3A7X1; -.
DR   STRING; 665007.ABB07_08015; -.
DR   PATRIC; fig|665007.5.peg.1754; -.
DR   Proteomes; UP000035366; Chromosome.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd13844; CuRO_1_BOD_CotA_like; 1.
DR   CDD; cd13869; CuRO_2_PHS; 1.
DR   CDD; cd13892; CuRO_3_PHS; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR   InterPro; IPR011707; Cu-oxidase-like_N.
DR   InterPro; IPR011706; Cu-oxidase_C.
DR   InterPro; IPR045087; Cu-oxidase_fam.
DR   InterPro; IPR033138; Cu_oxidase_CS.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   PANTHER; PTHR48267:SF1; BILIRUBIN OXIDASE; 1.
DR   PANTHER; PTHR48267; CUPREDOXIN SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 3.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   4: Predicted;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          71..106
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          480..610
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  69170 MW;  D39F8432FF953916 CRC64;
     MTDLIERTTG AAGQQADKEP DKTPVTDELT PYVAPLPVPP VLRPASADVL RETEIAIRPA
     WVRLHPQLPP TLMWGYDGQV PGPTIEVRRG QRVRIAWTNR IPKDSEYPVT SVEVPARAPG
     TPPPSTDPGR EGVEPDKDVA ALPAWTVTHL HGAQTGGGND GWADNAVGHG DAQLSEHPND
     HQAVQWWYHD HAMNITRWNV MTGLYGTYLV RDEEEDALRL PSGEREIPLL LADRNLDTDE
     DGRLNGRLLH KTVIVQQSNP ETGKPVSIPF TGPYTTVNGR IWPYTEVDAA WYRFRLVNAS
     NARIFELVLI DEDGNPVPGV VHQIGSDGGL LPRPVPVDFD GDLPTLTAAP AERFDLLVDF
     RALAGRTLRL VNKGPGQPAG VPDPAGNVRY PHVLEFRIRE TCAEDTFELP EVLSGSFRRL
     THDLPHGHRL ILLTPPATKG AGGHPEIWEL TEVGDPGGLT LPADGIVQVT GPDGTTRTYR
     RTSRTFNDGL GFTIAEGGYE QWSFLNLAPI VHPMHIHLAD FQLLGRDAYD VSGFDPAVGG
     TRTPIRYDAG RAIPLAPNER GNKDVFRVPG SQMLRVMGRF DGAYGRFMYH CHLLEHEDMG
     MMRPFVVMPA EAMRFDHGGT HGGHGEGHTG
//
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