HO2_SYNY3
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 03-AUG-2022, entry version 134.
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; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified 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 [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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15766254}.
CC -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
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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; 1148.1653304; -.
DR PaxDb; P74133; -.
DR EnsemblBacteria; BAA18219; BAA18219; BAA18219.
DR KEGG; syn:sll1875; -.
DR eggNOG; COG5398; Bacteria.
DR InParanoid; P74133; -.
DR OMA; ANRAFEY; -.
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:0055072; P:iron ion homeostasis; 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; -; 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 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
