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Entry version 78 (11 Dec 2019)
Sequence version 1 (17 Oct 2006)
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Protein

6-methylsalicylic acid synthase

Gene

atX

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Status
Reviewed-Annotation score:

Annotation score:4 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

6-methylsalicylic acid synthase; part of the gene cluster that mediates the biosynthesis of terreic acid, a quinone epoxide inhibitor of Bruton's tyrosine kinase (PubMed:24534845, PubMed:25265334). The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the 6-methylsalicylic acid synthase atX (PubMed:9003280, PubMed:9438344, PubMed:25265334). In the biosynthesis of 6-MSA, atX utilizes one acetyl-CoA and three malonyl-CoAs as its substrates and catalyzes a series of programmed reactions including Claisen condensation, dehydration, reduction, and cyclization to yield 6-MSA (PubMed:9003280, PubMed:9438344, PubMed:25265334). The 6-methylsalicylic acid decarboxylase atA then catalyzes the decarboxylative hydroxylation of 6-MSA to 3-methylcatechol (PubMed:25265334). The next step is the conversion of 3-methylcatechol to terremutin via several oxidation steps involving the cytochrome P450 monooxygenase atE and probably also the cytochrome P450 monooxygenase atG (PubMed:25265334). Lastly, atC is required for the oxidation of terremutin to terreic acid (PubMed:25265334). No function could be assigned to atD yet, although it is involved in the biosynthesis of terreic acid (PubMed:25265334).1 Publication3 Publications

<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 <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.1 Publication
View all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei216For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei667For malonyltransferase activityPROSITE-ProRule annotation1

<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

<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 functionAcyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase
LigandNADP

<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:
6-methylsalicylic acid synthase1 Publication (EC:2.3.1.1651 Publication)
Short name:
6-MSAS1 Publication
Alternative name(s):
Polyketide synthase atXCurated
Terreic acid biosynthesis protein X1 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:atX1 Publication
Synonyms:pksM1 Publication
ORF Names:ATEG_06275
<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>OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
<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 identifieri341663 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
<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
  • UP000007963 <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: Unassembled WGS sequence

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:ATEG_06275

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Terreic acid is a metabolite with antibiotic properties (PubMed:23686727). Terric acid acts also as a selective inhibitor of human Bruton's tyrosine kinase in mast cells and other immune cells (PubMed:10051623).2 Publications

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Abolishes the production of terreic acid (PubMed:25265334).1 Publication

<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_00004376331 – 18036-methylsalicylic acid synthaseAdd BLAST1803

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 residuei1761O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<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

Expression is observed in the middle of the vegetative growth phase (PubMed:9438344).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

STRING: functional protein association networks

More...
STRINGi
33178.CADATEAP00007925

<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
Q0CJ59

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

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>Domaini1726 – 1801CarrierPROSITE-ProRule annotationAdd BLAST76

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>Regioni47 – 473Ketosynthase (KS) domainSequence analysisAdd BLAST427
Regioni581 – 894Malonyl-CoA:ACP transacylase (MAT) domainSequence analysisAdd BLAST314
Regioni940 – 1214Dehydrogenase (DH) domainSequence analysisAdd BLAST275
Regioni1434 – 1628Ketoreductase (KR) domainSequence analysisAdd BLAST195

Phylogenomic databases

Identification of Orthologs from Complete Genome Data

More...
OMAi
IGTAYCG

Database of Orthologous Groups

More...
OrthoDBi
19161at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001227 Ac_transferase_dom_sf
IPR036736 ACP-like_sf
IPR014043 Acyl_transferase
IPR016035 Acyl_Trfase/lysoPLipase
IPR032821 KAsynt_C_assoc
IPR018201 Ketoacyl_synth_AS
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR016036 Malonyl_transacylase_ACP-bd
IPR036291 NAD(P)-bd_dom_sf
IPR020801 PKS_acyl_transferase
IPR020841 PKS_Beta-ketoAc_synthase_dom
IPR020807 PKS_dehydratase
IPR042104 PKS_dehydratase_sf
IPR013968 PKS_KR
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR016039 Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698 Acyl_transf_1, 1 hit
PF16197 KAsynt_C_assoc, 1 hit
PF00109 ketoacyl-synt, 1 hit
PF02801 Ketoacyl-synt_C, 1 hit
PF08659 KR, 1 hit
PF00550 PP-binding, 1 hit
PF14765 PS-DH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00827 PKS_AT, 1 hit
SM00826 PKS_DH, 1 hit
SM00825 PKS_KS, 1 hit
SM00823 PKS_PP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336 SSF47336, 1 hit
SSF51735 SSF51735, 2 hits
SSF52151 SSF52151, 1 hit
SSF53901 SSF53901, 1 hit
SSF55048 SSF55048, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00606 B_KETOACYL_SYNTHASE, 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.

Q0CJ59-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEVHGDEVLS VDSGVSTPPS TGSGFRRPLE TPGTEIGNLN LNPQNEVAVV
60 70 80 90 100
GMACRLAGGN NSPEELWQSI LNRKDASGEI PSMRWEPYYR RDIRNPKILD
110 120 130 140 150
QTTKRGYFLD HVENFDAAFF GVSPKEAEQM DPQQRLSLEV TWEALEDAGI
160 170 180 190 200
PPQSLSGSET AVFMGVNSDD YSKLLLEDIP NVEAWMGIGT AYCGVPNRIS
210 220 230 240 250
YHLNLMGPST AVDAACASSL VAIHHGRQAI LQGESEVAIV GGVNALCGPG
260 270 280 290 300
LTRVLDKAGA TSTEGRCLSF DEDAKGYGRG EGAAVVILKR LSTAIRDGDH
310 320 330 340 350
IRAIIKGSAV AQDGKTNGIM APNAKAQELV AWNALRTAGV DPLTVGYVEA
360 370 380 390 400
HATSTPLGDP TEVSAVSAVY GKGRPEGNPC FIGSVKPNVG HLEAGAGAVG
410 420 430 440 450
FIKAVMAVEK AIFPPQTNLK RLNSRIDWGQ AGVKVVQETL EWPGNEDDVR
460 470 480 490 500
RAGVCSYGYG GTVSHAIIEE FAQQLQRPTT NTTDEDPLPR ILLLSAPQER
510 520 530 540 550
RLALQARTQA SWIAAEGRNR TLESIATTLS TRRGHHDYRA AIIAENHDDA
560 570 580 590 600
VQKLSDIVNG KAAEWTTSSR VLDASCSKDV VWVFSGHGAQ WTAMATDLLK
610 620 630 640 650
DIVFYQTISR LDPIVEREMG FSALHSLASG DFESSIKVQV LTYLVQVGLA
660 670 680 690 700
AILRSKGLEP QAVIGHSVGE IAASVAAGCL TAEEGALIVT RRANLYRRVM
710 720 730 740 750
GAGAMVLVNI PFVDMEKELQ GRTDLVAAID SSPSSCVVSG ATEAVLALVE
760 770 780 790 800
DLKSRGVNAF RVKTDIPFHH PMLDQLSEPL REAMAGSLSP RKPRVRLYST
810 820 830 840 850
SAEDPRSMVA RDIYYWTSNM VNPVRLTAAV QAAVDDGLRL FLEVSSHPIV
860 870 880 890 900
SHSVRETMLD LGVEDFTVTN TMARNKPADK TILSSIAQLH CRGAVVNWKK
910 920 930 940 950
QLPGPWALDV PLTTWDHKPY WRHIHTGPIS ASTLHDVDKH TLLGQRVPVA
960 970 980 990 1000
GETTMVFTTQ MDDQTKPFPG SHPLHGSEIV PAAALVNTFL HATGATTLSN
1010 1020 1030 1040 1050
ITLRVPVAIS QPRDIQVVVS QNQIKICSRL TQKAGSGADE GSWLTHTTGQ
1060 1070 1080 1090 1100
WEAGGSKNAP AQLDIAAIKA RLANNKLADN FSIDYLDKVG VSAMGFPWAV
1110 1120 1130 1140 1150
TEHYGTLQEM IARVDVAPDV PATSPLPWDA ASWAPILDAA TSVGSTLFFD
1160 1170 1180 1190 1200
QPRLRMPAHI HGVQVYTTQP PLKVGYLYVE KAGDRDLAVH VSVCDELGTV
1210 1220 1230 1240 1250
LARFESMRFS EIEGTPGSNG SEESLVHQLA WPPAIYSEKP LTINNVVLVS
1260 1270 1280 1290 1300
RDKNVADLYC GSLKDRVSSI TVLDAAADLL SLSQDSSSVL QAKDTAVVYV
1310 1320 1330 1340 1350
PGPLHSADSI PTAAHSFLME LLLLVKIIVN GSLPTKVFVL TDRVCESESA
1360 1370 1380 1390 1400
TALAQSPIHG VSRIIAAEHP DQWGGLIDVE TPGQFPLETM KYVQEADNIR
1410 1420 1430 1440 1450
ISDGIPRIAR LRPLPRDKLL PPSKQTSLLP RPESTYLITG GLGALGLEVA
1460 1470 1480 1490 1500
QFLVEKGARR LILVSRRALP PRREWADILA DASSSLAPAL ETIQALEAQG
1510 1520 1530 1540 1550
ATVHTLAVDI SSPDAAPQLA VAIDSLSLPP VRGVVHAAGV LDSQLVLSAT
1560 1570 1580 1590 1600
SDSVERVLAP KITGALVLGT VFPPKALDFF MLFSSCGQLL GFPGQASYAS
1610 1620 1630 1640 1650
GNAFLDAFAT SRRHQGDNAV AVQWTSWRSL GMAASTDFIN AELASKGITD
1660 1670 1680 1690 1700
ITRDEGFRAW MHISKYDIDQ AAVLRSLAFE ADEPLPTPIL TDIAVRKAGS
1710 1720 1730 1740 1750
ASSADAPSAA PKETNEMPES IPERRTWLDE RIRDCVARVL QLGSSDEVDS
1760 1770 1780 1790 1800
KAALSDLGVD SVMTVSLRGQ LQKTLGVKVP PTLTWSCPTV SHLVGWFLEK

MGN
Length:1,803
Mass (Da):193,794
Last modified:October 17, 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:i302EF6DDA3A0E3C6
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
CH476602 Genomic DNA Translation: EAU32819.1

NCBI Reference Sequences

More...
RefSeqi
XP_001215453.1, XM_001215453.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
EAU32819; EAU32819; ATEG_06275

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4322099

<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
CH476602 Genomic DNA Translation: EAU32819.1
RefSeqiXP_001215453.1, XM_001215453.1

3D structure databases

SMRiQ0CJ59
ModBaseiSearch...

Protein-protein interaction databases

STRINGi33178.CADATEAP00007925

Genome annotation databases

EnsemblFungiiEAU32819; EAU32819; ATEG_06275
GeneIDi4322099

Organism-specific databases

EuPathDBiFungiDB:ATEG_06275

Phylogenomic databases

OMAiIGTAYCG
OrthoDBi19161at2759

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
InterProiView protein in InterPro
IPR001227 Ac_transferase_dom_sf
IPR036736 ACP-like_sf
IPR014043 Acyl_transferase
IPR016035 Acyl_Trfase/lysoPLipase
IPR032821 KAsynt_C_assoc
IPR018201 Ketoacyl_synth_AS
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR016036 Malonyl_transacylase_ACP-bd
IPR036291 NAD(P)-bd_dom_sf
IPR020801 PKS_acyl_transferase
IPR020841 PKS_Beta-ketoAc_synthase_dom
IPR020807 PKS_dehydratase
IPR042104 PKS_dehydratase_sf
IPR013968 PKS_KR
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR016039 Thiolase-like
PfamiView protein in Pfam
PF00698 Acyl_transf_1, 1 hit
PF16197 KAsynt_C_assoc, 1 hit
PF00109 ketoacyl-synt, 1 hit
PF02801 Ketoacyl-synt_C, 1 hit
PF08659 KR, 1 hit
PF00550 PP-binding, 1 hit
PF14765 PS-DH, 1 hit
SMARTiView protein in SMART
SM00827 PKS_AT, 1 hit
SM00826 PKS_DH, 1 hit
SM00825 PKS_KS, 1 hit
SM00823 PKS_PP, 1 hit
SUPFAMiSSF47336 SSF47336, 1 hit
SSF51735 SSF51735, 2 hits
SSF52151 SSF52151, 1 hit
SSF53901 SSF53901, 1 hit
SSF55048 SSF55048, 1 hit
PROSITEiView protein in PROSITE
PS00606 B_KETOACYL_SYNTHASE, 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 nameiATX_ASPTN
<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: Q0CJ59
<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 2, 2016
Last sequence update: October 17, 2006
Last modified: December 11, 2019
This is version 78 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

Keywords - Technical termi

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
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