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Database: UniProt
Entry: A0A1Z4RVF8_9CHRO
LinkDB: A0A1Z4RVF8_9CHRO
Original site: A0A1Z4RVF8_9CHRO 
ID   A0A1Z4RVF8_9CHRO        Unreviewed;       238 AA.
AC   A0A1Z4RVF8;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Heme oxygenase (Decyclizing) {ECO:0000313|EMBL:BAZ46450.1};
GN   Name=ho1 {ECO:0000313|EMBL:BAZ46450.1};
GN   ORFNames=NIES4102_34820 {ECO:0000313|EMBL:BAZ46450.1};
OS   Chondrocystis sp. NIES-4102.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Chondrocystis.
OX   NCBI_TaxID=2005460 {ECO:0000313|EMBL:BAZ46450.1, ECO:0000313|Proteomes:UP000217698};
RN   [1] {ECO:0000313|EMBL:BAZ46450.1, ECO:0000313|Proteomes:UP000217698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-4102 {ECO:0000313|EMBL:BAZ46450.1,
RC   ECO:0000313|Proteomes:UP000217698};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AP018281; BAZ46450.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4RVF8; -.
DR   KEGG; chon:NIES4102_34820; -.
DR   OrthoDB; 5493802at2; -.
DR   Proteomes; UP000217698; 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:UP000217698}.
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;  27275 MW;  69725258845F8D26 CRC64;
     MSIDLATMLR EGTKKSHTMA ENVGFVKCFL KGVVEKKSYR QLVTSLYFVY SAMEEEMEKL
     KDHPVISKIY FPELNRKQSL EQDLYFYYGA NWREEAKNTP AGKEYVARIR EIAKSQPELL
     VSHCYTRYLG DLSGGQILKK ISQRAMNLTD GKGTAFYEFE SIPDEKAFKD KYRQAMNDLP
     IDQATGEKIV NEANAAFGMN MKLFNELEGN LIKAIGIMLF NTLTRRRVRG STELVTAE
//
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