ID Q0IDM0_SYNS3 Unreviewed; 237 AA.
AC Q0IDM0;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Heme oxygenase {ECO:0000313|EMBL:ABI47778.1};
DE EC=1.14.99.3 {ECO:0000313|EMBL:ABI47778.1};
GN OrderedLocusNames=sync_0216 {ECO:0000313|EMBL:ABI47778.1};
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=64471 {ECO:0000313|EMBL:ABI47778.1, ECO:0000313|Proteomes:UP000001961};
RN [1] {ECO:0000313|EMBL:ABI47778.1, ECO:0000313|Proteomes:UP000001961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311 {ECO:0000313|EMBL:ABI47778.1,
RC ECO:0000313|Proteomes:UP000001961};
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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DR EMBL; CP000435; ABI47778.1; -; Genomic_DNA.
DR RefSeq; WP_011618200.1; NC_008319.1.
DR AlphaFoldDB; Q0IDM0; -.
DR STRING; 64471.sync_0216; -.
DR KEGG; syg:sync_0216; -.
DR eggNOG; COG5398; Bacteria.
DR HOGENOM; CLU_057050_2_0_3; -.
DR OrthoDB; 5493802at2; -.
DR Proteomes; UP000001961; 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 Oxidoreductase {ECO:0000313|EMBL:ABI47778.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001961}.
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; 26738 MW; 29C004C1BBE5C395 CRC64;
MSVALATQLR EGTKKSHTMA ENTGFVSCFL KGVVDKLSYR KLVADLFFVY EAMEEEMHRL
KEHPVLAPIA FEQLDRVTAL EEDLAFYFGT EWRQQIEASP AAKEYVARIR EVAQTAPELL
VGHHYTRYLG DLSGGQILKN IAQKAMNNPT DNGLHFYVFP EIADEKAFKT TYRSALDTLP
IDQAMADRIV EEANQAFHLN MKMFQELEGN LVAAIGKVLF GFLTRRQRTG STEAVVA
//
