ID A0A073CWZ2_PLAAG Unreviewed; 240 AA.
AC A0A073CWZ2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Ho1 {ECO:0000313|EMBL:KEI68560.1};
DE EC=1.14.99.3 {ECO:0000313|EMBL:KEI68560.1};
GN Name=ho1 {ECO:0000313|EMBL:KEI68560.1};
GN ORFNames=A19Y_3826 {ECO:0000313|EMBL:KEI68560.1};
OS Planktothrix agardhii NIVA-CYA 126/8.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI68560.1, ECO:0000313|Proteomes:UP000027395};
RN [1] {ECO:0000313|EMBL:KEI68560.1, ECO:0000313|Proteomes:UP000027395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI68560.1,
RC ECO:0000313|Proteomes:UP000027395};
RX PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(2014).
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DR EMBL; CM002803; KEI68560.1; -; Genomic_DNA.
DR RefSeq; WP_042155994.1; NZ_CM002803.1.
DR AlphaFoldDB; A0A073CWZ2; -.
DR STRING; 388467.A19Y_3826; -.
DR GeneID; 77289915; -.
DR PATRIC; fig|388467.6.peg.3772; -.
DR eggNOG; COG5398; Bacteria.
DR HOGENOM; CLU_057050_2_0_3; -.
DR Proteomes; UP000027395; 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:KEI68560.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027395}.
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 240 AA; 27457 MW; C7746E894FCD6F72 CRC64;
MSVNLATQLR EGTKKSHTMA ENVGFIKCFL KGTVEKTSYR KLVGNLYFVY SAMEEEMERH
RNHPILSKLY FPELNRKQSL EQDLYFYHGA NWKEEVQSSE TTKAYVARIR EISNSEPELL
IAHLYTRYLG DLSGGQILKG IAQNAMNLQD GQGTQFYEFN DIPDEKAFKV NYRQQMDSVD
IDQEMATCIV DEANDAFGMN MKMFNELEGN LVKAIGQMLF NTLTRRRTKG ATEGLATAAE
//
