HO1_SYNY3
ID HO1_SYNY3 Reviewed; 240 AA.
AC P72849;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Heme oxygenase 1;
DE EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
GN Name=pbsA1; OrderedLocusNames=sll1184;
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 (2.5 ANGSTROMS) IN COMPLEX WITH HEME, AND
RP IRON-BINDING SITE.
RX PubMed=15560792; DOI=10.1111/j.1432-1033.2004.04411.x;
RA Sugishima M., Migita C.T., Zhang X., Yoshida T., Fukuyama K.;
RT "Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis
RT sp. PCC 6803 in complex with heme.";
RL Eur. J. Biochem. 271:4517-4525(2004).
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 -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
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DR EMBL; BA000022; BAA16864.1; -; Genomic_DNA.
DR PIR; S74713; S74713.
DR PDB; 1WE1; X-ray; 2.50 A; A/B/C/D=1-240.
DR PDBsum; 1WE1; -.
DR AlphaFoldDB; P72849; -.
DR SMR; P72849; -.
DR IntAct; P72849; 2.
DR STRING; 1148.1651938; -.
DR PaxDb; P72849; -.
DR EnsemblBacteria; BAA16864; BAA16864; BAA16864.
DR KEGG; syn:sll1184; -.
DR eggNOG; COG5398; Bacteria.
DR InParanoid; P72849; -.
DR OMA; KKSHTMA; -.
DR PhylomeDB; P72849; -.
DR BioCyc; MetaCyc:MON-13860; -.
DR BRENDA; 1.14.14.18; 6192.
DR BRENDA; 1.14.15.20; 382.
DR EvolutionaryTrace; P72849; -.
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..240
FT /note="Heme oxygenase 1"
FT /id="PRO_0000209701"
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 HELIX 5..12
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 36..59
FT /evidence="ECO:0007829|PDB:1WE1"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 120..146
FT /evidence="ECO:0007829|PDB:1WE1"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 182..205
FT /evidence="ECO:0007829|PDB:1WE1"
FT HELIX 207..222
FT /evidence="ECO:0007829|PDB:1WE1"
SQ SEQUENCE 240 AA; 27051 MW; 7F17A033768BAFA8 CRC64;
MSVNLASQLR EGTKKSHSMA ENVGFVKCFL KGVVEKNSYR KLVGNLYFVY SAMEEEMAKF
KDHPILSHIY FPELNRKQSL EQDLQFYYGS NWRQEVKISA AGQAYVDRVR QVAATAPELL
VAHSYTRYLG DLSGGQILKK IAQNAMNLHD GGTAFYEFAD IDDEKAFKNT YRQAMNDLPI
DQATAERIVD EANDAFAMNM KMFNELEGNL IKAIGIMVFN SLTRRRSQGS TEVGLATSEG
