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UniProtKB - A0A0S2E7W7 (INVA5_PAXIN)

Entry version 14 (08 May 2019)
Sequence version 1 (17 Feb 2016)
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Protein

Atromentin synthetase invA5

Gene

invA5

Organism
Paxillus involutus (Naked brimcap)
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

An L-tyrosine:2-oxoglutarate aminotransferase (probably invD) and atromentin synthetase invA5 catalyze consecutive steps to turn over L-tyrosine into atromentin, which represents the generic precursor molecule for the entire terphenylquinone and pulvinic acid family of pigments, which are widely distributed secondary metabolites in homobasidiomycetes. The first step catalyzed by the aminotransferase converts L-tyrosine in to 4-hydroxyphenylpyruvate (4-HPP). Adenylation of two 4-HPP monomers by the invA5 adenylation (A) domain, covalent tethering of the monomers as a thioester and oxoester onto the invA5 thiolation (T) and thioesterase (TE) domains, respectively, and symmetric C-C-bond formation between two monomers catalyzed by the invA5 TE domain leads to atromentin.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>pH dependencei

Optimum pH is 7.4.1 Publication

Temperature dependencei

Optimum temperature is 25 degrees Celsius.1 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: Secondary metabolite biosynthesis

This protein is involved in Secondary metabolite biosynthesis.By similarity
View all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.

<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 functionTransferase

<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:
Atromentin synthetase invA5 (EC:2.3.1.-)
Alternative name(s):
Nonribosomal peptide synthase-like enzyme invA5
Short name:
NRPS-like
<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:invA5
<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>OrganismiPaxillus involutus (Naked brimcap)
<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 identifieri71150 [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 lineageiEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetidae › Boletales › Paxilineae › Paxillaceae › Paxillus

<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_00004426251 – 953Atromentin synthetase invA5Add BLAST953

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei629O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini592 – 670CarrierPROSITE-ProRule annotationAdd BLAST79

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>Regioni37 – 460Adenylation (A) domainSequence analysisAdd BLAST424
Regioni597 – 667Thiolation and peptide carrier (T) domainSequence analysisAdd BLAST71
Regioni693 – 795Thioesterase (TE) domainSequence analysisAdd BLAST103

<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 ATP-dependent AMP-binding enzyme family.Curated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1200.10, 1 hit
3.40.50.12780, 1 hit
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029058 AB_hydrolase
IPR036736 ACP-like_sf
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
IPR020802 PKS_thioesterase
IPR009081 PP-bd_ACP
IPR001031 Thioesterase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00501 AMP-binding, 1 hit
PF00550 PP-binding, 1 hit
PF00975 Thioesterase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00824 PKS_TE, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47336 SSF47336, 1 hit
SSF53474 SSF53474, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00455 AMP_BINDING, 1 hit
PS50075 CARRIER, 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.

A0A0S2E7W7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTPIAITPVA PVDIIYDLKH TERATESSPV TLLDVFSRAV SQYPDHELSF 
        60         70         80         90        100
ITSSAHDSTV HTKTFAEFNQ HVHALAQAMR AWGKPTGSVI VVYLTEHEDN 
       110        120        130        140        150
MAAVWASLLA GYVPCLQPAL SAQQAHKEGH VGHIKNLFSS ATWLTNESGA 
       160        170        180        190        200
EQVQSISGLD IHLLSELKAS AEAGVDFQAH QPNPDDEAIL FLTSGSTGFS 
       210        220        230        240        250
KAVVHTHRTI LAACHAKGES YGLTSESKIM NWVGFDHVAG SLEMHIAPLL 
       260        270        280        290        300
YGASQLHVHA SAILSDPLRF LHLIEEKSIQ LAFAPNFLLA KLTRDLEKRS 
       310        320        330        340        350
DLFGKFDLSS IKRINSGGEA VVSSTAQAFA RTLQNLAKDG DASFVISAGF 
       360        370        380        390        400
GMTETCAGCI YDPINVLETP PSYEFLELGT PVAGCEMRIV NPEDGVTPRP 
       410        420        430        440        450
DGESGELQVR GPMVFVRYYN NPEATSSSFV EGGWYRTGDV GIVEQGKMRL 
       460        470        480        490        500
SGRIKDTVIV HGVSYGIPEL ETYLQTVEGV THSFLAAAPY RAPGQETEGF 
       510        520        530        540        550
VVFYSPTFDL DSEDAPAKLF ATHRALRDVS VKLITLPPQQ IIPIPINQME 
       560        570        580        590        600
KTTLGKLSRA RLVNLLKQGE LAKHIDRAEE LVSIARGASF VAPSTETEKT 
       610        620        630        640        650
LAGIYAGIFN LSVSDMSASE NFFELGGTSI DVIRLKREGE SAFDLPEIPT 
       660        670        680        690        700
IQILKHPVIS SLAKYVDSLI SKDASQEEYD PIVPLQLTGN KTPIFMVHPG 
       710        720        730        740        750
VGEVLIFVNL AKYFQNERPF YALRARGFEP GHPFFTTMDE MVSCYAAAVK 
       760        770        780        790        800
RTQPHGPYAI AGYSYGGVVA FEVAKRLEAM GDEVKFTGLI NIPPNIADRM 
       810        820        830        840        850
HEIDWTGGML NLSYFLGLVS KQDANDLAPS MRPLTRKEQL EIVWKLSPPE 
       860        870        880        890        900
RLVELQLTPE KLDHWVDIAG SLIECGKTYE PGSSVSVLDV FYAIPLRGSK 
       910        920        930        940        950
EDWLNKQLKP WAGYSRAEPS YTDVPGQHYT LMDFDHVPGF QKIFRSRLEA 

RGL
Length:953
Mass (Da):104,609
Last modified:February 17, 2016 - 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:i531CBAC5B156DF29
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
KT958233 mRNA Translation: ALN66885.1

<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
KT958233 mRNA Translation: ALN66885.1

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

More...SWISS-MODEL-Workspacei		Submit a new modelling project...

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.40.50.12780, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR036736 ACP-like_sf
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
IPR020802 PKS_thioesterase
IPR009081 PP-bd_ACP
IPR001031 Thioesterase
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF00550 PP-binding, 1 hit
PF00975 Thioesterase, 1 hit
SMARTiView protein in SMART
SM00824 PKS_TE, 1 hit
SUPFAMiSSF47336 SSF47336, 1 hit
SSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit
PS50075 CARRIER, 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 nameiINVA5_PAXIN
<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: A0A0S2E7W7
<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: December 20, 2017
Last sequence update: February 17, 2016
Last modified: May 8, 2019
This is version 14 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 programFungal 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

Documents

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