ID A0A0J5P5M9_9PAST Unreviewed; 515 AA.
AC A0A0J5P5M9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Bilirubin oxidase {ECO:0000313|EMBL:KMK50774.1};
GN ORFNames=RO21_09845 {ECO:0000313|EMBL:KMK50774.1};
OS Muribacter muris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Muribacter.
OX NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK50774.1, ECO:0000313|Proteomes:UP000036270};
RN [1] {ECO:0000313|EMBL:KMK50774.1, ECO:0000313|Proteomes:UP000036270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK50774.1,
RC ECO:0000313|Proteomes:UP000036270};
RA Christensen H., Nicklas W., Bisgaard M.;
RT "Reclassification of Actinobacillus muris as Muribacter muris.";
RL Submitted (DEC-2014) 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:KMK50774.1}.
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DR EMBL; JWIZ01000069; KMK50774.1; -; Genomic_DNA.
DR RefSeq; WP_047977617.1; NZ_JWIZ01000069.1.
DR AlphaFoldDB; A0A0J5P5M9; -.
DR STRING; 67855.RO21_09845; -.
DR PATRIC; fig|67855.3.peg.2079; -.
DR Proteomes; UP000036270; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13855; CuRO_1_McoC_like; 1.
DR CDD; cd13881; CuRO_2_McoC_like; 1.
DR CDD; cd13902; CuRO_3_McoC_like; 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; IPR002355; Cu_oxidase_Cu_BS.
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.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000036270};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..515
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005262692"
FT DOMAIN 83..196
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 400..515
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 515 AA; 58645 MW; 0642A9255B69480C CRC64;
MKRRDFLRYG IGISLASSSL YSLANMMNHA QHGNMAMMHS VPTGLMPTEA MPSGLSLNGI
LPKLANQSTQ AGLFKATLKA EPIKIRLADN KETEFWAYNG QLPGPQIEVF EGDTVEIEFI
NHLPQPSTVH WHGLDVPNEA DGNPMDMVEP QGKKVYRFTL PQGSAGTYWY HPHPHDHVSE
QVYKGLAGTF VVKAKNDPLA HLPEQHWVIS DLRLNADGTI PANTMLDWMN GREGEFVLIN
GQYQPQIQVK TNERIRLWNA TSARYFRLNI PGVKWIVVGT EGGLLEKPRS PVDELLLTPA
ERVEVIMVGE TQGTVNLQSG YYDRRKMMVQ EQPKDLTLAT IQVKSEPVQL PESLRSLPNW
DEPKQVRQIR FSEKMMNHTN MPMMNHGTHH ATTTPTDNPI PPMMNGMFLI NGQTFDMNRI
DFVTKLNEVE QWEIFNESHM DHPFHLHGTQ FEVIQHTLNG KTFKPEGRAL KDVVNLRPYE
KVIIRFKQGH TGLKMYHCHI LEHENLGMMG MFKVE
//
