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UniProtKB - B5GW45 (TMUUS_STRCL)

Entry version 54 (29 Sep 2021)
Sequence version 1 (14 Oct 2008)
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Protein

(+)-T-muurolol synthase ((2E,6E)-farnesyl diphosphate cyclizing)

Gene

SCLAV_p0068

Organism
Streptomyces clavuligerus
Status
Reviewed-Annotation score:

Annotation score:3 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

Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (+)-T-muurolol via a 1,10-cyclization, which requires isomerization of FPP to nerolidyl diphosphate (NPP) and then abstraction of the pyrophosphate from intermediate NPP leading to a (E,Z)-germacradienyl (helminthogermacradienyl) cation.

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 3 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

kcat is 0.00163 sec(-1).1 Publication
  1. KM=2.7 µM for (2E,6E)-farnesyl diphosphate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: terpenoid biosynthesis

This protein is involved in the pathway terpenoid biosynthesis, which is part of Secondary metabolite biosynthesis.By similarity
View all proteins of this organism that are known to be involved in the pathway terpenoid biosynthesis and in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei80Plays a critical role in the stabilization of intermediate cationBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi83Magnesium 1By similarity1
Sitei84Plays a critical role for substrate recognitionBy similarity1
Metal bindingi88Magnesium 1By similarity1
Metal bindingi88Magnesium 2By similarity1
Sitei159Plays a critical role for substrate recognitionBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei179SubstrateBy similarity1
Sitei183Plays a critical role for abstraction of the pyrophosphate groupBy similarity1
Metal bindingi225Magnesium 3By similarity1
Metal bindingi229Magnesium 3By similarity1
Binding sitei232SubstrateBy similarity1
Metal bindingi233Magnesium 3By 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionLyase
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		4.2.3.98, 5988

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

More...UniPathwayi		UPA00213

<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%5Fand%5Ftaxonomy%5Fsection">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:
(+)-T-muurolol synthase ((2E,6E)-farnesyl diphosphate cyclizing)1 Publication (EC:4.2.3.981 Publication)
Alternative name(s):
Terpene cyclase1 Publication
Type I terpene synthase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
ORF Names:SCLAV_p0068, SSCG_03688
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlasmid pSCL41 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiStreptomyces clavuligerus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri1901 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Actinobacteria › Streptomycetales › Streptomycetaceae › Streptomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002357 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Plasmid pSCL4
  • UP000006569 Componenti: Unassembled WGS sequence

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004184781 – 418(+)-T-muurolol synthase ((2E,6E)-farnesyl diphosphate cyclizing)Add BLAST418

<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		443255.SCLAV_p0068

<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		B5GW45

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>Regioni312 – 313Substrate bindingBy similarity2
Regioni354 – 418DisorderedSequence analysisAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi83 – 88DDXXXD motifBy similarity6

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The Asp-Asp-Xaa-Xaa-Xaa-Asp (DDXXXD) motif is important for the catalytic activity, presumably through binding to Mg2+.By similarity

<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 terpene synthase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG3170, Bacteria

Identification of Orthologs from Complete Genome Data

More...OMAi		AMEHWVI

Database of Orthologous Groups

More...OrthoDBi		1869158at2

Family and domain databases

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
IPR034686, Terpene_cyclase-like_2

Structure-Function Linkage Database

More...SFLDi		SFLDG01020, Terpene_Cyclase_Like_2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48576, SSF48576, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

B5GW45-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLNHSDLMF YCPVDDLPHP AASGVNDRTL DWASGQGIPT ADRDAGRLRA 
        60         70         80         90        100
MAPGLLAARI APDARGPVLD AFADHHTWLF AFDDEYCDRA DGSGITEWAS 
       110        120        130        140        150
FLARLHRVVE TGESALLPGN PYGLALRDIA CRLSTYTTPA QLAEWLEALR 
       160        170        180        190        200
SYFAALVWER SRRRDDDRLQ SLDDYLLLRL RNGAMHTSIT LLDTVNGYVL 
       210        220        230        240        250
PRELRETPGV RALVEMTALL VSVDNDILSH HKESTSGTRE ANLLDVLGRT 
       260        270        280        290        300
GHTTPGEAVA QAVALRNEIM RQFVRVAERV RTPAAVPELY RFTTGLARWI 
       310        320        330        340        350
RANLDFSLTT TRYTGPVTER AALSPHEVPP LSGQGPAPAR SDVIGWWWRI 
       360        370        380        390        400
PEPLPEPGSD GADTPVRKRR AGDRPPTAGR GGAPHHQRTG PPPPVLPGGI 
       410 
TASRSSGLQQ STWRREHR
Length:418
Mass (Da):46,002
Last modified:October 14, 2008 - 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:iC0F63991CF0F4C1E
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
CM000914 Genomic DNA Translation: EFG03561.2
DS570654 Genomic DNA Translation: EDY50541.1

NCBI Reference Sequences

More...RefSeqi		WP_003956090.1, NZ_CP027859.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		EDY50541; EDY50541; SSCG_03688

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ag:EFG03561

<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
CM000914 Genomic DNA Translation: EFG03561.2
DS570654 Genomic DNA Translation: EDY50541.1
RefSeqiWP_003956090.1, NZ_CP027859.1

3D structure databases

SMRiB5GW45
ModBaseiSearch...

Protein-protein interaction databases

STRINGi443255.SCLAV_p0068

Genome annotation databases

EnsemblBacteriaiEDY50541; EDY50541; SSCG_03688
KEGGiag:EFG03561

Phylogenomic databases

eggNOGiCOG3170, Bacteria
OMAiAMEHWVI
OrthoDBi1869158at2

Enzyme and pathway databases

UniPathwayiUPA00213
BRENDAi4.2.3.98, 5988

Family and domain databases

Gene3Di1.10.600.10, 1 hit
InterProiView protein in InterPro
IPR008949, Isoprenoid_synthase_dom_sf
IPR034686, Terpene_cyclase-like_2
SFLDiSFLDG01020, Terpene_Cyclase_Like_2, 1 hit
SUPFAMiSSF48576, SSF48576, 1 hit

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 nameiTMUUS_STRCL
<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: B5GW45
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: October 14, 2008
Last modified: September 29, 2021
This is version 54 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

Plasmid, 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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