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P72849 (HO1_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heme oxygenase 1

EC=1.14.99.3
Gene names
Name:pbsA1
Ordered Locus Names:sll1184
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the opening of the heme ring with the release of iron. Key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae By similarity.

Catalytic activity

Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

Sequence similarities

Belongs to the heme oxygenase family.

Ontologies

Keywords
   Biological processPhotosynthesis
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processheme oxidation

Inferred from electronic annotation. Source: InterPro

photosynthesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionheme oxygenase (decyclizing) activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Heme oxygenase 1
PRO_0000209701

Sites

Metal binding171Iron (heme axial ligand)

Secondary structure

............................... 240
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P72849 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 7F17A033768BAFA8

FASTA24027,051
        10         20         30         40         50         60 
MSVNLASQLR EGTKKSHSMA ENVGFVKCFL KGVVEKNSYR KLVGNLYFVY SAMEEEMAKF 

        70         80         90        100        110        120 
KDHPILSHIY FPELNRKQSL EQDLQFYYGS NWRQEVKISA AGQAYVDRVR QVAATAPELL 

       130        140        150        160        170        180 
VAHSYTRYLG DLSGGQILKK IAQNAMNLHD GGTAFYEFAD IDDEKAFKNT YRQAMNDLPI 

       190        200        210        220        230        240 
DQATAERIVD EANDAFAMNM KMFNELEGNL IKAIGIMVFN SLTRRRSQGS TEVGLATSEG 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.
[2]"Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme."
Sugishima M., Migita C.T., Zhang X., Yoshida T., Fukuyama K.
Eur. J. Biochem. 271:4517-4525(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH HEME, IRON-BINDING SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA16864.1.
PIRS74713.
RefSeqNP_440184.1. NC_000911.1.
YP_005650241.1. NC_017277.1.
YP_007450067.1. NC_020286.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WE1X-ray2.50A/B/C/D1-240[»]
ProteinModelPortalP72849.
SMRP72849. Positions 2-223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP72849. 2 interactions.
STRING1148.sll1184.

Proteomic databases

PaxDbP72849.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA16864; BAA16864; BAA16864.
GeneID12255928.
14615712.
953483.
KEGGsyn:sll1184.
syy:SYNGTS_0288.
syz:MYO_12900.
PATRIC23837492. VBISynSp132158_0318.

Phylogenomic databases

eggNOGCOG5398.
HOGENOMHOG000233221.
KOK00510.
OMAKKSHTMA.
OrthoDBEOG69PQ2G.
PhylomeDBP72849.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13860.

Family and domain databases

Gene3D1.20.910.10. 1 hit.
InterProIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERPTHR10720. PTHR10720. 1 hit.
PfamPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFPIRSF000343. Haem_Oase. 1 hit.
PRINTSPR00088. HAEMOXYGNASE.
SUPFAMSSF48613. SSF48613. 1 hit.
PROSITEPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP72849.

Entry information

Entry nameHO1_SYNY3
AccessionPrimary (citable) accession number: P72849
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references