Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 119 (11 Dec 2019)
Sequence version 1 (01 Feb 1997)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Apocarotenoid-15,15'-oxygenase

Gene

sll1541

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cleaves a number of carotenals and carotenols in the all-trans configuration at the 15-15' double bond producing retinal or retinol, respectively. Also shows activity toward lycopenals and the corresponding alcohols. Does not cleave beta-carotene or lycopene.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=2.5 µM for 8'-apo-beta-carotenal1 Publication
  2. KM=43 µM for 8'-apo-beta-carotenol1 Publication
  3. KM=1.4 µM for (3R)-3-OH-8'-apo-beta-carotenal1 Publication
  4. KM=31 µM for (3R)-3-OH-8'-apo-beta-carotenol1 Publication
  5. KM=2.6 µM for (3R)-3-OH-12'-apo-beta-carotenal1 Publication
  1. Vmax=40 pmol/min/mg enzyme with 8'-apo-beta-carotenal as substrate1 Publication
  2. Vmax=650 pmol/min/mg enzyme with 8'-apo-beta-carotenol as substrate1 Publication
  3. Vmax=71 pmol/min/mg enzyme with (3R)-3-OH-8'-apo-beta-carotenal as substrate1 Publication
  4. Vmax=705 pmol/min/mg enzyme with (3R)-3-OH-8'-apo-beta-carotenol as substrate1 Publication
  5. Vmax=11.5 pmol/min/mg enzyme with (3R)-3-OH-12'-apo-beta-carotenal as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi183Iron; catalytic1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei206Substrate; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi238Iron; catalytic1 Publication1
Binding sitei303Substrate1 Publication1
Metal bindingi304Iron; catalytic1 Publication1
Metal bindingi484Iron; catalytic1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDioxygenase, Oxidoreductase
LigandIron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-15972

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.13.11.75 6192

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P74334

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Apocarotenoid-15,15'-oxygenase
Short name:
ACO
Alternative name(s):
8'-apo-beta-carotenal 15,15'-oxygenase (EC:1.13.11.75)
Diox1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Ordered Locus Names:sll1541
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1111708 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystisunclassified Synechocystis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001425 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB02253 (1r)-4-[(1e,3e,5e,7z,9e,11z,13e,15e)-17-Hydroxy-3,7,12,16-Tetramethylheptadeca-1,3,5,7,9,11,13,15-Octaen-1-Yl]-3,5,5-Trimethylcyclohex-3-En-1-Ol
DB04233 (Hydroxyethyloxy)Tri(Ethyloxy)Octane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003875671 – 490Apocarotenoid-15,15'-oxygenaseAdd BLAST490

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P74334

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By high light.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P74334, 2 interactors

STRING: functional protein association networks

More...
STRINGi
1148.1653515

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1490
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P74334

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P74334

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the carotenoid oxygenase family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000254835

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P74334

KEGG Orthology (KO)

More...
KOi
K00464

Identification of Orthologs from Complete Genome Data

More...
OMAi
HHIPYGL

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P74334

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004294 Carotenoid_Oase

The PANTHER Classification System

More...
PANTHERi
PTHR10543 PTHR10543, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03055 RPE65, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P74334-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVTSPPTSSP SQRSYSPQDW LRGYQSQPQE WDYWVEDVEG SIPPDLQGTL
60 70 80 90 100
YRNGPGLLEI GDRPLKHPFD GDGMVTAFKF PGDGRVHFQS KFVRTQGYVE
110 120 130 140 150
EQKAGKMIYR GVFGSQPAGG WLKTIFDLRL KNIANTNITY WGDRLLALWE
160 170 180 190 200
GGQPHRLEPS NLATIGLDDL GGILAEGQPL SAHPRIDPAS TFDGGQPCYV
210 220 230 240 250
TFSIKSSLSS TLTLLELDPQ GKLLRQKTET FPGFAFIHDF AITPHYAIFL
260 270 280 290 300
QNNVTLNGLP YLFGLRGAGE CVQFHPDKPA QIILVPRDGG EIKRIPVQAG
310 320 330 340 350
FVFHHANAFE ENGKIILDSI CYNSLPQVDT DGDFRSTNFD NLDPGQLWRF
360 370 380 390 400
TIDPAAATVE KQLMVSRCCE FPVVHPQQVG RPYRYVYMGA AHHSTGNAPL
410 420 430 440 450
QAILKVDLES GTETLRSFAP HGFAGEPIFV PRPGGVAEDD GWLLCLIYKA
460 470 480 490
DLHRSELVIL DAQDITAPAI ATLKLKHHIP YPLHGSWAQT
Length:490
Mass (Da):54,286
Last modified:February 1, 1997 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF72AD2AAE81E6F25
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BA000022 Genomic DNA Translation: BAA18428.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S76169

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
BAA18428; BAA18428; BAA18428

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
syn:sll1541

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA Translation: BAA18428.1
PIRiS76169

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BIWX-ray2.39A/B/C/D1-490[»]
2BIXX-ray2.68A/B1-490[»]
4OU8X-ray2.80A/B/C/D1-490[»]
4OU9X-ray2.00A/B/C/D1-490[»]
5KJAX-ray2.80A/B/C/D/E1-490[»]
5KJBX-ray2.81A/B/C/D/E1-490[»]
5KJDX-ray2.75A/B/C/D/E1-490[»]
5KK0X-ray2.80A/B/C/D1-490[»]
6BIGX-ray2.21A/B/C/D1-490[»]
6C7KX-ray2.50A/B/C/D1-490[»]
6C7OX-ray3.15A/B1-490[»]
6C7PX-ray2.60A/B1-490[»]
SMRiP74334
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP74334, 2 interactors
STRINGi1148.1653515

Chemistry databases

DrugBankiDB02253 (1r)-4-[(1e,3e,5e,7z,9e,11z,13e,15e)-17-Hydroxy-3,7,12,16-Tetramethylheptadeca-1,3,5,7,9,11,13,15-Octaen-1-Yl]-3,5,5-Trimethylcyclohex-3-En-1-Ol
DB04233 (Hydroxyethyloxy)Tri(Ethyloxy)Octane

Proteomic databases

PaxDbiP74334

Genome annotation databases

EnsemblBacteriaiBAA18428; BAA18428; BAA18428
KEGGisyn:sll1541

Phylogenomic databases

HOGENOMiHOG000254835
InParanoidiP74334
KOiK00464
OMAiHHIPYGL
PhylomeDBiP74334

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15972
BRENDAi1.13.11.75 6192
SABIO-RKiP74334

Miscellaneous databases

EvolutionaryTraceiP74334

Family and domain databases

InterProiView protein in InterPro
IPR004294 Carotenoid_Oase
PANTHERiPTHR10543 PTHR10543, 1 hit
PfamiView protein in Pfam
PF03055 RPE65, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACOX_SYNY3
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P74334
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: February 1, 1997
Last modified: December 11, 2019
This is version 119 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again