ID HO2_SYNY3 Reviewed; 250 AA. AC P74133; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 141. DE RecName: Full=Heme oxygenase 2; DE EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782}; GN Name=pbsA2; OrderedLocusNames=sll1875; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH HEME, SUBUNIT, AND RP IRON-BINDING SITE. RX PubMed=15766254; DOI=10.1021/bi0480483; RA Sugishima M., Hagiwara Y., Zhang X., Yoshida T., Migita C.T., Fukuyama K.; RT "Crystal structure of dimeric heme oxygenase-2 from Synechocystis sp. PCC RT 6803 in complex with heme."; RL Biochemistry 44:4257-4266(2005). 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. {ECO:0000250}. 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:0000250|UniProtKB:O48782}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15766254}. CC -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000022; BAA18219.1; -; Genomic_DNA. DR PIR; S75658; S75658. DR PDB; 1WOV; X-ray; 1.75 A; A/B=1-250. DR PDB; 1WOW; X-ray; 2.20 A; A/B=1-250. DR PDB; 1WOX; X-ray; 2.10 A; A/B=1-250. DR PDBsum; 1WOV; -. DR PDBsum; 1WOW; -. DR PDBsum; 1WOX; -. DR AlphaFoldDB; P74133; -. DR SMR; P74133; -. DR IntAct; P74133; 2. DR STRING; 1148.gene:10499092; -. DR PaxDb; 1148-1653304; -. DR EnsemblBacteria; BAA18219; BAA18219; BAA18219. DR KEGG; syn:sll1875; -. DR eggNOG; COG5398; Bacteria. DR InParanoid; P74133; -. DR PhylomeDB; P74133; -. DR EvolutionaryTrace; P74133; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0020037; F:heme binding; IBA:GO_Central. DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042167; P:heme catabolic process; IBA:GO_Central. DR GO; GO:0006788; P:heme oxidation; IBA:GO_Central. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; Heme; Iron; Metal-binding; Oxidoreductase; Photosynthesis; KW Reference proteome. FT CHAIN 1..250 FT /note="Heme oxygenase 2" FT /id="PRO_0000209702" FT REGION 228..250 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 16 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 HELIX 4..11 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 13..20 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 23..30 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 35..58 FT /evidence="ECO:0007829|PDB:1WOV" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 63..68 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 71..73 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 76..87 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 91..94 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 99..114 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 119..130 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 133..144 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 164..180 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 185..207 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 210..217 FT /evidence="ECO:0007829|PDB:1WOV" FT HELIX 219..226 FT /evidence="ECO:0007829|PDB:1WOV" FT STRAND 243..247 FT /evidence="ECO:0007829|PDB:1WOV" SQ SEQUENCE 250 AA; 28540 MW; F3F54814D51709FC CRC64; MTNLAQKLRY GTQQSHTLAE NTAYMKCFLK GIVEREPFRQ LLANLYYLYS ALEAALRQHR DNEIISAIYF PELNRTDKLA EDLTYYYGPN WQQIIQPTPC AKIYVDRLKT IAASEPELLI AHCYTRYLGD LSGGQSLKNI IRSALQLPEG EGTAMYEFDS LPTPGDRRQF KEIYRDVLNS LPLDEATINR IVEEANYAFS LNREVMHDLE DLIKAAIGEH TFDLLTRQDR PGSTEARSTA GHPITLMVGE //