ID   A0A2C6CT63_9BACT        Unreviewed;       612 AA.
AC   A0A2C6CT63;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Bilirubin oxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CEQ90_13750 {ECO:0000313|EMBL:PHI19272.1};
OS   Lewinellaceae bacterium SD302.
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae.
OX   NCBI_TaxID=2014804 {ECO:0000313|EMBL:PHI19272.1, ECO:0000313|Proteomes:UP000223945};
RN   [1] {ECO:0000313|EMBL:PHI19272.1, ECO:0000313|Proteomes:UP000223945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD302 {ECO:0000313|EMBL:PHI19272.1,
RC   ECO:0000313|Proteomes:UP000223945};
RA   Wang K.;
RT   "The draft genome sequence of Lewinellaceae bacterium SD302.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHI19272.1}.
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DR   EMBL; PDLQ01000021; PHI19272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C6CT63; -.
DR   OrthoDB; 9757546at2; -.
DR   Proteomes; UP000223945; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR008972; Cupredoxin.
DR   PANTHER; PTHR11709:SF218; FI03373P-RELATED; 1.
DR   PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 3.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000223945};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..612
FT                   /note="Bilirubin oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013333409"
FT   DOMAIN          85..179
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          391..518
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   612 AA;  67535 MW;  1F50254851DDA01E CRC64;
     MMAMFSTTFL RRLLTAGLLL LTVSLAAQEF VNPFYTPPQA VTGFGYISLD KISTTHNFSP
     MGSDSLNVGV STYAYEDFNS PGTTTILGPT LVWQYQDNLT LDVLNRLDEP SGIYFQGVNA
     VAHQIGGVQN TIAPDGLTEY SFKIENKPTT LWYHPLVPGE TAEQVQRGFG GMIIVEDQNV
     DATLSFWHDV FPTNYGVDDI PVIVQTKKFR RNEAGVIEIQ ADQGYNADYT YLVNGSVDPV
     LNVGADMIRL RFLNADAKFA FNLGVTSDLA GQNTQDLQLI AVDGGYTTQS RTKSEVLVGA
     GETFEVLIDL RGLEGQTFYL FNRVSAMPDG VIGNSTTTSG YATDRALMKI EVGPSTTISP
     IIGFPLNIYF DPDRPSQTEV SNTRMKVLRQ DPLPAGNIYN VDSVQLDTND VIDIVMQDSV
     EVWTIDNTTD IAHPWHLHGF KFWVTEIMEN GTPLDLFDYP EITDGPQTSV FIRPGWTLSY
     ITRFNDFGTQ VSKDSSYLFQ SGNLQHFDKG MAGQFVVWNG EESPSSLNNP NTTPRDMELF
     PNPTAGTLHL KGNSAKASIL HVLDINGRLL REIRLAPFQG STELNVSGLP AGTLVLDWRS
     AEGRAVRRVT LH
//