ID   A0A3P1WMY1_9ACTN        Unreviewed;       209 AA.
AC   A0A3P1WMY1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Biliverdin-producing heme oxygenase {ECO:0000313|EMBL:RRD47912.1};
GN   ORFNames=EII42_01305 {ECO:0000313|EMBL:RRD47912.1};
OS   Tessaracoccus sp. OH4464_COT-324.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=2491059 {ECO:0000313|EMBL:RRD47912.1, ECO:0000313|Proteomes:UP000274803};
RN   [1] {ECO:0000313|EMBL:RRD47912.1, ECO:0000313|Proteomes:UP000274803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OH4464_COT-324 {ECO:0000313|EMBL:RRD47912.1,
RC   ECO:0000313|Proteomes:UP000274803};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-2018) 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:RRD47912.1}.
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; RQYZ01000001; RRD47912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P1WMY1; -.
DR   OrthoDB; 5493802at2; -.
DR   Proteomes; UP000274803; Unassembled WGS sequence.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006788; P:heme oxidation; IEA:InterPro.
DR   CDD; cd19165; HemeO; 1.
DR   Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR   InterPro; IPR002051; Haem_Oase.
DR   InterPro; IPR016053; Haem_Oase-like.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   PANTHER; PTHR10720; HEME OXYGENASE; 1.
DR   PANTHER; PTHR10720:SF0; HEME OXYGENASE; 1.
DR   Pfam; PF01126; Heme_oxygenase; 1.
DR   PIRSF; PIRSF000343; Haem_Oase; 1.
DR   PRINTS; PR00088; HAEMOXYGNASE.
DR   SUPFAM; SSF48613; Heme oxygenase-like; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|PIRSR:PIRSR000343-1};
KW   Iron {ECO:0000256|PIRSR:PIRSR000343-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000343-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274803}.
FT   BINDING         10
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT   BINDING         17
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000343-2"
FT   BINDING         125
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT   BINDING         171
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ   SEQUENCE   209 AA;  23880 MW;  BD15AE54D8912A29 CRC64;
     MSTPLSELVR SQTRVQHDAA ERSPLMTELV EGAALKTHLE LQVQLWFIYE ALESRLDAWR
     NYPEIAAFHD PRLNRLPAIA TSFSAVWGTG WRDQLRANPE TLDYAADIRL CADQLDGPRF
     LAHHYTRYLG DLSGGRIIGR NLQRATGAAD EVVGFYSFPD LKPKPFKDEY RARLDSLPWD
     EAGRETFLAA VRDSYVLNER MFRGILNAR
//