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Database: UniProt
Entry: A0A1J0PA82_9SYNE
LinkDB: A0A1J0PA82_9SYNE
Original site: A0A1J0PA82_9SYNE 
ID   A0A1J0PA82_9SYNE        Unreviewed;       237 AA.
AC   A0A1J0PA82;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Heme oxygenase {ECO:0000313|EMBL:APD48143.1};
GN   ORFNames=BM449_07660 {ECO:0000313|EMBL:APD48143.1};
OS   Synechococcus sp. SynAce01.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1916956 {ECO:0000313|EMBL:APD48143.1, ECO:0000313|Proteomes:UP000182608};
RN   [1] {ECO:0000313|Proteomes:UP000182608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SynAce01 {ECO:0000313|Proteomes:UP000182608};
RA   Tang J., Daroch M., Liang Y., Jiang D., Shah M.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP018091; APD48143.1; -; Genomic_DNA.
DR   RefSeq; WP_071800776.1; NZ_CP018091.1.
DR   AlphaFoldDB; A0A1J0PA82; -.
DR   STRING; 1916956.BM449_07660; -.
DR   KEGG; syny:BM449_07660; -.
DR   OrthoDB; 5493802at2; -.
DR   Proteomes; UP000182608; Chromosome.
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:UP000182608}.
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         173
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ   SEQUENCE   237 AA;  26304 MW;  118E8E6016DB7ACD CRC64;
     MSVALASQLR EGTKKAHTMA ENTGFVTCFL KGVVDKSSYR KLVADLYFVY CAMEEEIGKL
     KSHPVVGPIA SDALNRRSSL EADLEFYFGS DWRSTVQPTS AAQEYVARLH QVAQETPELL
     VGHHYTRYIG DLSGGVILKN IAQKAMNLGE HEGLRFYEFD AIPDEKVFKA AYRQSLDALP
     IDQAMADQIV AEANHAFHLN MTMFQELEGN LVAAIGKLLF GFLTRRQRAG STEPVVA
//
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