ID   HO1_NOSS1               Reviewed;         238 AA.
AC   Q8YVS7;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Heme oxygenase 1;
DE            EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
GN   Name=pbsA1; OrderedLocusNames=all1897;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
RN   [2]
RP   FUNCTION.
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=16452471; DOI=10.1074/jbc.m513796200;
RA   Zhao K.H., Su P., Li J., Tu J.M., Zhou M., Bubenzer C., Scheer H.;
RT   "Chromophore attachment to phycobiliprotein beta-subunits:
RT   phycocyanobilin:cysteine-beta84 phycobiliprotein lyase activity of CpeS-
RT   like protein from Anabaena Sp. PCC7120.";
RL   J. Biol. Chem. 281:8573-8581(2006).
CC   -!- FUNCTION: Catalyzes the opening of the heme ring with the release of
CC       iron. Key enzyme in the synthesis of the chromophoric part of the
CC       photosynthetic antennae (By similarity). Upon overexpression in E.coli
CC       with PCB:ferredoxin oxidoreductase, CpeS and either CpcB or PecB
CC       permits synthesis of phycocyanin-coupled CpcB or PecB. {ECO:0000250,
CC       ECO:0000269|PubMed:16452471}.
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 [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:60344; EC=1.14.14.18;
CC         Evidence={ECO:0000250|UniProtKB:O48782};
CC   -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
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DR   EMBL; BA000019; BAB73596.1; -; Genomic_DNA.
DR   PIR; AC2043; AC2043.
DR   RefSeq; WP_010996061.1; NZ_RSCN01000017.1.
DR   AlphaFoldDB; Q8YVS7; -.
DR   SMR; Q8YVS7; -.
DR   STRING; 103690.17130987; -.
DR   PRIDE; Q8YVS7; -.
DR   EnsemblBacteria; BAB73596; BAB73596; BAB73596.
DR   KEGG; ana:all1897; -.
DR   eggNOG; COG5398; Bacteria.
DR   OMA; KKSHTMA; -.
DR   OrthoDB; 1371367at2; -.
DR   BioCyc; MetaCyc:MON-18996; -.
DR   Proteomes; UP000002483; 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   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   CDD; cd19165; HemeO; 1.
DR   Gene3D; 1.20.910.10; -; 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; PTHR10720; 1.
DR   Pfam; PF01126; Heme_oxygenase; 1.
DR   PIRSF; PIRSF000343; Haem_Oase; 1.
DR   PRINTS; PR00088; HAEMOXYGNASE.
DR   SUPFAM; SSF48613; SSF48613; 1.
DR   PROSITE; PS00593; HEME_OXYGENASE; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Oxidoreductase; Photosynthesis;
KW   Reference proteome.
FT   CHAIN           1..238
FT                   /note="Heme oxygenase 1"
FT                   /id="PRO_0000403173"
SQ   SEQUENCE   238 AA;  26902 MW;  D28DA4EEC4DA79BD CRC64;
     MSSNLANKLR VGTKKAHTMA ENVGFVKCFL KGVVEKSSYR KLVANFYYVY SAMEEEMEKH
     SQHPIVSKIN FSQLNRKQTL EQDLSYYYGA NWREQIQLSP AGEAYVQRIR EISATEPELL
     IAHSYTRYLG DLSGGQILKN IAVTAMNLND GQGTAFYEFA DISDEKAFKA KYRQTLDELA
     IDEATGDRIV DEANAAFGMN MKMFQELEGN LIKAIGMMLF NTLTRKRTRG ATELATAE