ID K9V881_9CYAN Unreviewed; 238 AA.
AC K9V881;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Heme oxygenase {ECO:0000313|EMBL:AFZ03455.1};
DE EC=1.14.99.3 {ECO:0000313|EMBL:AFZ03455.1};
GN ORFNames=Cal6303_4555 {ECO:0000313|EMBL:AFZ03455.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ03455.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFZ03455.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ03455.1,
RC ECO:0000313|Proteomes:UP000010477};
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003610; AFZ03455.1; -; Genomic_DNA.
DR RefSeq; WP_015200072.1; NC_019751.1.
DR AlphaFoldDB; K9V881; -.
DR STRING; 1170562.Cal6303_4555; -.
DR KEGG; calt:Cal6303_4555; -.
DR PATRIC; fig|1170562.3.peg.4977; -.
DR eggNOG; COG5398; Bacteria.
DR HOGENOM; CLU_057050_2_0_3; -.
DR OrthoDB; 5493802at2; -.
DR Proteomes; UP000010477; 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:AFZ03455.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010477}.
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 238 AA; 26798 MW; 10B18C21C3842615 CRC64;
MSSNLASKLR IGTKKAHTMA ENVGFVKCFL KGVVEKTSYR KLVANFYFVY SAMEEEMDKH
KNHPIVGKIN FPQLNRKQSL EEDLTYYYGA NWRDQIKVSP AGAAYVERIR KISATAPELL
ISHSYTRYMG DLSGGQILKG IAQNAMNLSD GDGTAFYEFP EISDEKAFKA NYRAALDEMP
LDEATCDRIV EEANDAFGVN MKMFQELEGN LVKAIGQMLF NTLTRRRTRG STELATAE
//
