ID B7K4H5_RIPO1 Unreviewed; 238 AA.
AC B7K4H5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=heme oxygenase (biliverdin-producing) {ECO:0000256|ARBA:ARBA00012360};
DE EC=1.14.14.18 {ECO:0000256|ARBA:ARBA00012360};
GN OrderedLocusNames=PCC8801_1380 {ECO:0000313|EMBL:ACK65440.1};
OS Rippkaea orientalis (strain PCC 8801 / RF-1) (Cyanothece sp. (strain PCC
OS 8801)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX NCBI_TaxID=41431 {ECO:0000313|EMBL:ACK65440.1, ECO:0000313|Proteomes:UP000008204};
RN [1] {ECO:0000313|Proteomes:UP000008204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 8801 {ECO:0000313|Proteomes:UP000008204};
RX PubMed=21972240; DOI=10.1128/mBio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18;
CC Evidence={ECO:0000256|ARBA:ARBA00001701};
CC -!- SIMILARITY: Belongs to the heme oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006134}.
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DR EMBL; CP001287; ACK65440.1; -; Genomic_DNA.
DR RefSeq; WP_012594714.1; NC_011726.1.
DR AlphaFoldDB; B7K4H5; -.
DR STRING; 41431.PCC8801_1380; -.
DR KEGG; cyp:PCC8801_1380; -.
DR eggNOG; COG5398; Bacteria.
DR HOGENOM; CLU_057050_2_0_3; -.
DR OrthoDB; 5493802at2; -.
DR Proteomes; UP000008204; Chromosome.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-EC.
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 InterPro; IPR018207; Haem_oxygenase_CS.
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.
DR PROSITE; PS00593; HEME_OXYGENASE; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000343-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000343-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000343-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACK65440.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008204}.
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; 27108 MW; DCEF8EA84CB635B0 CRC64;
MSVNLATMLR EGTKKSHSMA ENVGFVKCFL KGVVEKNSYR KLVANLYFVY SAMEEEMDKL
KDHEIVSKIY FPQLHRKHSL EKDLYYYYGA NWRNEIVLSE AGEAYVQRIH ELANSAPELL
VAHSYTRYLG DLSGGQILKK IAERAMNLGE DGGTAFYEFP TISDEKAFKN KYRQSLNELP
IDQTTADRIV DEANAAFGMN MKMFQELEGN LIKAIGIMLF NTLTRRRTTG STELATAD
//
