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Entry version 84 (11 Dec 2019)
Sequence version 1 (21 Mar 2006)
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Protein

4,4'-diapophytoene synthase

Gene

crtM

Organism
Staphylococcus aureus (strain NCTC 8325)
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

Involved in the biosynthesis of the yellow-orange carotenoid staphyloxanthin, which plays a role in the virulence via its protective function against oxidative stress. Catalyzes the head-to-head condensation of two molecules of farnesyl diphosphate (FPP) into the colorless C(30) carotenoid 4,4'-diapophytoene (dehydrosqualene).3 Publications

Miscellaneous

CrtM is not functional in a C(40) pathway, however independent mutations on Phe-26, Trp-38 or Glu-180 are sufficient to permit the synthesis of C(40) carotenoids, such as lycopene and 3,4,3',4'-tetrahydrolycopene, although there is a decrease in the synthesis of C(30) compounds. The combination of mutations at Phe-26 and Trp-38 appears to be harmful for the general performance of the enzyme.1 Publication
Upon coexpression with Erwinia geranylgeranyldiphosphate (GGDP) synthase, CrtM produces novel carotenoids with the asymmetrical C(35) backbone, such as 4-apophytoene, and the production of the natural product 4,4'-diapophytoene drops dramatically.1 Publication

<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

Mg2+By similarityNote: Binds 2 Mg2+ ions per subunit.By similarity

<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=1.2 µM for farnesyl diphosphate1 Publication
  1. Vmax=176 µM/h/mg enzyme1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: staphyloxanthin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes staphyloxanthin from farnesyl diphosphate.1 Publication
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. 4,4'-diapophytoene synthase (crtM)
  2. 4,4'-diapophytoene desaturase (4,4'-diaponeurosporene-forming) (crtN)
  3. 4,4'-diaponeurosporene oxygenase (crtP)
  4. 4,4'-diaponeurosporenoate glycosyltransferase (crtQ)
  5. Glycosyl-4,4'-diaponeurosporenoate acyltransferase (crtO)
This subpathway is part of the pathway staphyloxanthin biosynthesis, which is itself part of Carotenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes staphyloxanthin from farnesyl diphosphate, the pathway staphyloxanthin biosynthesis and in Carotenoid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei41Farnesyl diphosphate 1By similarity1
Binding sitei45Farnesyl diphosphate 1By similarity1
Binding sitei45Farnesyl diphosphate 2By similarity1
<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 bindingi48Magnesium 1By similarity1
Metal bindingi52Magnesium 1By similarity1
Binding sitei165Farnesyl diphosphate 2By similarity1
Metal bindingi168Magnesium 2By similarity1
Binding sitei171Farnesyl diphosphate 1By similarity1
Metal bindingi172Magnesium 2By similarity1
Binding sitei248Farnesyl diphosphate 1By similarity1

<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 functionTransferase
Biological processCarotenoid biosynthesis, Virulence
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
GCF_000013425:G1I0R-2710-MONOMER
SAUR93061:G1G5Y-2710-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q2FV59

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00029;UER00556

<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:
4,4'-diapophytoene synthase1 Publication (EC:2.5.1.962 Publications)
Short name:
DAP synthase1 Publication
Alternative name(s):
C30 carotenoid synthase1 Publication
Dehydrosqualene synthase1 Publication
<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
Name:crtM1 Publication
Ordered Locus Names:SAOUHSC_02879
<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>OrganismiStaphylococcus aureus (strain NCTC 8325)
<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 identifieri93061 [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 lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
<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
  • UP000008816 <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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi26F → A, G, L or S: Decrease in C(30) carotene synthase activity. C(40) carotene synthase activity acquired. 2 Publications1
Mutagenesisi26F → A: Decrease in C(30) and C(40) carotene synthase activities; when associated with A-38 or G-38. 2 Publications1
Mutagenesisi26F → G: Decrease in C(30) and C(40) carotene synthase activities; when associated with A-38 or G-38. 2 Publications1
Mutagenesisi38W → A: Decrease in C(30) and C(40) carotene synthase activities; when associated with A-26 or G-26. 2 Publications1
Mutagenesisi38W → C: Decrease in C(30) carotene synthase activity. C(40) carotene synthase activity acquired. 2 Publications1
Mutagenesisi38W → G: Decrease in C(30) and C(40) carotene synthase activities; when associated with A-26 or G-26. 2 Publications1
Mutagenesisi180E → G: Slight increase in C(30) carotene synthase activity. C(40) carotene synthase activity acquired. 2 Publications1

<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_00002826161 – 2874,4'-diapophytoene synthaseAdd BLAST287

<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

STRING: functional protein association networks

More...
STRINGi
1280.SAXN108_2813

<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

3D structure databases

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

More...
SMRi
Q2FV59

Database of comparative protein structure models

More...
ModBasei
Search...

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni18 – 21Farnesyl diphosphate 1 bindingBy similarity4

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105FE1 Bacteria
COG1562 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000220848

KEGG Orthology (KO)

More...
KOi
K10208

Identification of Orthologs from Complete Genome Data

More...
OMAi
MIAGQRM

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00683 Trans_IPPS_HH, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.600.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008949 Isoprenoid_synthase_dom_sf
IPR002060 Squ/phyt_synthse
IPR019845 Squalene/phytoene_synthase_CS
IPR033904 Trans_IPPS_HH

Structure-Function Linkage Database

More...
SFLDi
SFLDG01018 Squalene/Phytoene_Synthase_Lik, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48576 SSF48576, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01044 SQUALEN_PHYTOEN_SYN_1, 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.

Q2FV59-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTMMDMNFKY CHKIMKKHSK SFSYAFDLLP EDQRKAVWAI YAVCRKIDDS
60 70 80 90 100
IDVYGDIQFL NQIKEDIQSI EKYPYEHHHF QSDRRIMMAL QHVAQHKNIA
110 120 130 140 150
FQSFYNLIDT VYKDQHFTMF ETDAELFGYC YGVAGTVGEV LTPILSDHET
160 170 180 190 200
HQTYDVARRL GESLQLINIL RDVGEDFDNE RIYFSKQRLK QYEVDIAEVY
210 220 230 240 250
QNGVNNHYID LWEYYAAIAE KDFQDVMDQI KVFSIEAQPI IELAARIYIE
260 270 280
ILDEVRQANY TLHERVFVDK RKKAKLFHEI NSKYHRI
Length:287
Mass (Da):34,231
Last modified:March 21, 2006 - 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:i2407009413D42E63
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CP000253 Genomic DNA Translation: ABD31876.1

NCBI Reference Sequences

More...
RefSeqi
WP_000178307.1, NZ_LS483365.1
YP_501333.1, NC_007795.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABD31876; ABD31876; SAOUHSC_02879

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3921549

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sao:SAOUHSC_02879

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|93061.5.peg.2602

<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
CP000253 Genomic DNA Translation: ABD31876.1
RefSeqiWP_000178307.1, NZ_LS483365.1
YP_501333.1, NC_007795.1

3D structure databases

SMRiQ2FV59
ModBaseiSearch...

Protein-protein interaction databases

STRINGi1280.SAXN108_2813

Genome annotation databases

EnsemblBacteriaiABD31876; ABD31876; SAOUHSC_02879
GeneIDi3921549
KEGGisao:SAOUHSC_02879
PATRICifig|93061.5.peg.2602

Phylogenomic databases

eggNOGiENOG4105FE1 Bacteria
COG1562 LUCA
HOGENOMiHOG000220848
KOiK10208
OMAiMIAGQRM

Enzyme and pathway databases

UniPathwayiUPA00029;UER00556
BioCyciGCF_000013425:G1I0R-2710-MONOMER
SAUR93061:G1G5Y-2710-MONOMER
SABIO-RKiQ2FV59

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q2FV59

Family and domain databases

CDDicd00683 Trans_IPPS_HH, 1 hit
Gene3Di1.10.600.10, 1 hit
InterProiView protein in InterPro
IPR008949 Isoprenoid_synthase_dom_sf
IPR002060 Squ/phyt_synthse
IPR019845 Squalene/phytoene_synthase_CS
IPR033904 Trans_IPPS_HH
SFLDiSFLDG01018 Squalene/Phytoene_Synthase_Lik, 1 hit
SUPFAMiSSF48576 SSF48576, 1 hit
PROSITEiView protein in PROSITE
PS01044 SQUALEN_PHYTOEN_SYN_1, 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 nameiCRTM_STAA8
<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: Q2FV59
<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: April 3, 2007
Last sequence update: March 21, 2006
Last modified: December 11, 2019
This is version 84 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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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