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UniProtKB - Q12053 (AFLC_ASPPU)

Entry version 120 (23 Feb 2022)
Sequence version 1 (01 Nov 1997)
Previous versions | rss
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Protein

Norsolorinic acid synthase

Gene

aflC

Organism
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)
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

Norsolorinic acid synthase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:7592391, PubMed:15094053, PubMed:7565588, PubMed:15006741).

The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741).

The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits aflA and aflB, as well as the PKS aflC (PubMed:15006741).

AflC combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (PubMed:17086560, PubMed:18403714).

The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase aflA/aflB (PubMed:16256699).

The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin (PubMed:10584035).

The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN (PubMed:15006741).

The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) (PubMed:8368836).

The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway (PubMed:15006741, PubMed:11055914, PubMed:15932995).

The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA) (PubMed:15006741).

VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL) (PubMed:15006741).

Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen (PubMed:15006741, PubMed:8368837, PubMed:15932995).

Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA) (PubMed:15006741, PubMed:8368837).

A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2 (PubMed:15006741).

Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST) (PubMed:15006741, PubMed:1339261, PubMed:15771506).

AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring (PubMed:16332900, PubMed:16461654).

The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST) (PubMed:10543813).

Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively (PubMed:8434913).

Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 (PubMed:15006741, PubMed:11996570, PubMed:15528514, PubMed:18486503).

2 Publications20 Publications

<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

pantetheine 4'-phosphate1 PublicationNote: Binds 1 phosphopantetheine covalently.1 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: aflatoxin biosynthesis

This protein is involved in the pathway aflatoxin biosynthesis, which is part of Mycotoxin biosynthesis.1 Publication1 Publication
View all proteins of this organism that are known to be involved in the pathway aflatoxin biosynthesis and in Mycotoxin biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei543For beta-ketoacyl synthase activityBy similarity1
Active sitei993For acyl/malonyl transferase activityBy similarity1
Active sitei1937For thioesterase activity1 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

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 functionAcyltransferase, Multifunctional enzyme, Transferase

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.1.221, 523

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

More...UniPathwayi		UPA00287

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...ESTHERi		aspor-PKSL1, Thioesterase

<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:
Norsolorinic acid synthase1 Publication (EC:2.3.1.2212 Publications)
Short name:
NSAS1 Publication
Alternative name(s):
Aflatoxin biosynthesis polyketide synthaseCurated
Aflatoxin biosynthesis protein C1 Publication
Polyketide synthase A1 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
Name:aflC1 Publication
Synonyms:pksA1 Publication, pksL11 Publication
ORF Names:P875_00052995
<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>OrganismiAspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)
<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 identifieri1403190 [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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus ›
<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
  • UP000033540 <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: Unassembled WGS sequence

<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 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

Impairs the production of norsolorinic acid, as well as of the four major forms of aflatoxin: AFB1, AFB2, AFG1 and AFG2 (PubMed:7592391, PubMed:7565588).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi1345H → A: Abolishes catalytic activity. 1 Publication1
Mutagenesisi1491G → L: Abolishes catalytic activity. 1 Publication1
Mutagenesisi1543D → A: Abolishes catalytic activity. 1 Publication1
Mutagenesisi1546T → A: 40% decrease in catalytic activity. 1 Publication1
Mutagenesisi1547Q → A: Abolishes catalytic activity. 1 Publication1
Mutagenesisi1554N → A: Abolishes catalytic activity. 1 Publication1
Mutagenesisi1937S → A: Abolishes hydrolytic activity. 1 Publication1
Mutagenesisi1964D → N: Abolishes hydrolytic activity. 1 Publication1
Mutagenesisi2070D → N: Slight reduction in hydrolytic activity. 1 Publication1
Mutagenesisi2088H → F: Abolishes hydrolytic activity. 1 Publication1

<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_00001803031 – 2109Norsolorinic acid synthaseAdd BLAST2109

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 residuei1746O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1 Publication1

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

Actively expressed at 27 degrees Celsius but not at all at a temperature higher than 35 degrees Celsius (PubMed:7592391). Expression is repressed by curcumin (PubMed:23113196).2 Publications

<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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Q12053
With#Exp.IntAct
itself4EBI-15811477,EBI-15811477

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-59286N

STRING: functional protein association networks

More...STRINGi		1403190.Q12053

<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

12109
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q12053

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

More...SMRi		Q12053

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		Q12053

<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%5Fand%5Fdomains%5Fsection">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>Domaini1709 – 1788CarrierPROSITE-ProRule annotation1 PublicationAdd BLAST80

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>Regioni1 – 374Starter unit:ACP transacylase (SAT) domainSequence analysisAdd BLAST374
Regioni363 – 819Ketoacyl synthase (KS)domainSequence analysis1 PublicationAdd BLAST457
Regioni895 – 1216Malonyl-CoA:ACP transacylase (MAT) domainSequence analysis1 PublicationAdd BLAST322
Regioni1206 – 1713Product template (PT) domainSequence analysisAdd BLAST508
Regioni1281 – 1300DisorderedSequence analysisAdd BLAST20
Regioni1669 – 1707DisorderedSequence analysisAdd BLAST39
Regioni1789 – 1844DisorderedSequence analysisAdd BLAST56
Regioni1867 – 2102Thioesterase/Claisen cyclase (TE/CLC) domainSequence analysisAdd BLAST236

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1669 – 1688Polar residuesSequence analysisAdd BLAST20
Compositional biasi1797 – 1824Polar residuesSequence analysisAdd BLAST28

<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 domain architecture includes starter unit:ACP transacylase (SAT), beta-ketoacyl synthase (KS), malonyl-CoA:ACP transacylase (MAT), product template (PT), acyl-carrier domain (ACP), and thioesterase/Claisen cyclase (TE/CLC) domains (PubMed:17086560). The SAT domain receives a C6-fatty acid starter unit and transfers it onto the ACP for chain elongation. The KS accepts the hexanoyl-ACP unit and subsequent malonate extender units are loaded onto the ACP from the MAT domain for chain extension to generate the linear poly-beta-keto ACP-bound intermediate. The linear intermediate is then cyclized and aromatized in the PT domain. The resulting bicyclic intermediate is ultimately transferred from the ACP to the TE/CLC domain and undergoes Claisen-type C-C bond cyclization to release the product norsolorinic acid anthrone (noranthrone), which spontaneously oxidizes in vitro to norsolorinic acid (PubMed:17086560, PubMed:18403714, PubMed:19847268, PubMed:20332208).4 Publications

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, 2 hits
3.40.47.10, 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
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR030918, PT_fungal_PKS
IPR032088, SAT
IPR001031, Thioesterase
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
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit
PF16073, SAT, 1 hit
PF00975, Thioesterase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00827, PKS_AT, 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
SSF52151, SSF52151, 1 hit
SSF53474, SSF53474, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR04532, PT_fungal_PKS, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
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%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.

Q12053-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAQSRQLFLF GDQTADFVPK LRSLLSVQDS PILAAFLDQS HYVVRAQMLQ 
        60         70         80         90        100
SMNTVDHKLA RTADLRQMVQ KYVDGKLTPA FRTALVCLCQ LGCFIREYEE 
       110        120        130        140        150
SGNMYPQPSD SYVLGFCMGS LAAVAVSCSR SLSELLPIAV QTVLIAFRLG 
       160        170        180        190        200
LCALEMRDRV DGCSDDRGDP WSTIVWGLDP QQARDQIEVF CRTTNVPQTR 
       210        220        230        240        250
RPWISCISKN AITLSGSPST LRAFCAMPQM AQHRTAPIPI CLPAHNGALF 
       260        270        280        290        300
TQADITTILD TTPTTPWEQL PGQIPYISHV TGNVVQTSNY RDLIEVALSE 
       310        320        330        340        350
TLLEQVRLDL VETGLPRLLQ SRQVKSVTIV PFLTRMNETM SNILPDSFIS 
       360        370        380        390        400
TETRTDTGRA IPASGRPGAG KCKLAIVSMS GRFPESPTTE SFWDLLYKGL 
       410        420        430        440        450
DVCKEVPRRR WDINTHVDPS GKARNKGATK WGCWLDFSGD FDPRFFGISP 
       460        470        480        490        500
KEAPQMDPAQ RMALMSTYEA MERAGLVPDT TPSTQRDRIG VFHGVTSNDW 
       510        520        530        540        550
METNTAQNID TYFITGGNRG FIPGRINFCF EFAGPSYTND TACSSSLAAI 
       560        570        580        590        600
HLACNSLWRG DCDTAVAGGT NMIYTPDGHT GLDKGFFLSR TGNCKPYDDK 
       610        620        630        640        650
ADGYCRAEGV GTVFIKRLED ALADNDPILG VILDAKTNHS AMSESMTRPH 
       660        670        680        690        700
VGAQIDNMTA ALNTTGLHPN DFSYIEMHGT GTQVGDAVEM ESVLSVFAPS 
       710        720        730        740        750
ETARKADQPL FVGSAKANVG HGEGVSGVTS LIKVLMMMQH DTIPPHCGIK 
       760        770        780        790        800
PGSKINRNFP DLGARNVHIA FEPKPWPRTH TPRRVLINNF SAAGGNTALI 
       810        820        830        840        850
VEDAPERHWP TEKDPRSSHI VALSAHVGAS MKTNLERLHQ YLLKNPHTDL 
       860        870        880        890        900
AQLSYTTTAR RWHYLHRVSV TGASVEEVTR KLEMAIQNGD GVSRPKSKPK 
       910        920        930        940        950
ILFAFTGQGS QYATMGKQVY DAYPSFREDL EKFDRLAQSH GFPSFLHVCT 
       960        970        980        990       1000
SPKGDVEEMA PVVVQLAITC LQMALTNLMT SFGIRPDVTV GHSLGEFAAL 
      1010       1020       1030       1040       1050
YAAGVLSASD VVYLVGQRAE LLQERCQRGT HAMLAVKATP EALSQWIQDH 
      1060       1070       1080       1090       1100
DCEVACINGP EDTVLSGTTK NVAEVQRAMT DNGIKCTLLK LPFAFHSAQV 
      1110       1120       1130       1140       1150
QPILDDFEAL AQGATFAKPQ LLILSPLLRT EIHEQGVVTP SYVAQHCRHT 
      1160       1170       1180       1190       1200
VDMAQALRSA REKGLIDDKT LVIELGPKPL ISGMVKMTLG DKISTLPTLA 
      1210       1220       1230       1240       1250
PNKAIWPSLQ KILTSVYTGG WDINWKKYHA PFASSQKVVD LPSYGWDLKD 
      1260       1270       1280       1290       1300
YYIPYQGDWC LHRHQQDCKC AAPGHEIKTA DYQVPPESTP HRPSKLDPSK 
      1310       1320       1330       1340       1350
EAFPEIKTTT TLHRVVEETT KPLGATLVVE TDISRKDVNG LARGHLVDGI 
      1360       1370       1380       1390       1400
PLCTPSFYAD IAMQVGQYSM QRLRAGHPGA GAIDGLVDVS DMVVDKALVP 
      1410       1420       1430       1440       1450
HGKGPQLLRT TLTMEWPPKA AATTRSAKVK FATYFADGKL DTEHASCTVR 
      1460       1470       1480       1490       1500
FTSDAQLKSL RRSVSEYKTH IRQLHDGHAK GQFMRYNRKT GYKLMSSMAR 
      1510       1520       1530       1540       1550
FNPDYMLLDY LVLNEAENEA ASGVDFSLGS SEGTFAAHPA HVDAITQVAG 
      1560       1570       1580       1590       1600
FAMNANDNVD IEKQVYVNHG WDSFQIYQPL DNSKSYQVYT KMGQAKENDL 
      1610       1620       1630       1640       1650
VHGDVVVLDG EQIVAFFRGL TLRSVPRGAL RVVLQTTVKK ADRQLGFKTM 
      1660       1670       1680       1690       1700
PSPPPPTTTM PISPYKPANT QVSSQAIPAE ATHSHTPPQP KHSPVPETAG 
      1710       1720       1730       1740       1750
SAPAAKGVGV SNEKLDAVMR VVSEESGIAL EELTDDSNFA DMGIDSLSSM 
      1760       1770       1780       1790       1800
VIGSRFREDL GLDLGPEFSL FIDCTTVRAL KDFMLGSGDA GSGSNVEDPP 
      1810       1820       1830       1840       1850
PSATPGINPE TDWSSSASDS IFASEDHGHS SESGADTGSP PALDLKPYCR 
      1860       1870       1880       1890       1900
PSTSVVLQGL PMVARKTLFM LPDGGGSAFS YASLPRLKSD TAVVGLNCPY 
      1910       1920       1930       1940       1950
ARDPENMNCT HGAMIESFCN EIRRRQPRGP YHLGGWSSGG AFAYVVAEAL 
      1960       1970       1980       1990       2000
VNQGEEVHSL IIIDAPIPQA MEQLPRAFYE HCNSIGLFAT QPGASPDGST 
      2010       2020       2030       2040       2050
EPPSYLIPHF TAVVDVMLDY KLAPLHARRM PKVGIVWAAD TVMDERDAPK 
      2060       2070       2080       2090       2100
MKGMHFMIQK RTEFGPDGWD TIMPGASFDI VRADGANHFT LMQKEHVSII 

SDLIDRVMA
Length:2,109
Mass (Da):230,716
Last modified:November 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:iCB701372A16D8551
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
L42766 mRNA Translation: AAC41675.1
L42765 Genomic DNA Translation: AAC41674.1
AY371490 Genomic DNA Translation: AAS66004.1
JZEE01000728 Genomic DNA Translation: KJK60793.1

Protein sequence database of the Protein Information Resource

More...PIRi		T17490

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		KJK60793; KJK60793; P875_00052995

<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
L42766 mRNA Translation: AAC41675.1
L42765 Genomic DNA Translation: AAC41674.1
AY371490 Genomic DNA Translation: AAS66004.1
JZEE01000728 Genomic DNA Translation: KJK60793.1
PIRiT17490

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
2KR5NMR-A1705-1791[»]
3HRQX-ray1.80A/B1305-1660[»]
3HRRX-ray1.90A/B1305-1660[»]
3ILSX-ray1.70A1845-2109[»]
5KBZX-ray1.80A/B1305-1660[»]
BMRBiQ12053
SMRiQ12053
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-59286N
STRINGi1403190.Q12053

Protein family/group databases

ESTHERiaspor-PKSL1, Thioesterase

Genome annotation databases

EnsemblFungiiKJK60793; KJK60793; P875_00052995

Enzyme and pathway databases

UniPathwayiUPA00287
BRENDAi2.3.1.221, 523

Miscellaneous databases

EvolutionaryTraceiQ12053

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 2 hits
3.40.47.10, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR030918, PT_fungal_PKS
IPR032088, SAT
IPR001031, Thioesterase
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
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit
PF16073, SAT, 1 hit
PF00975, Thioesterase, 1 hit
SMARTiView protein in SMART
SM00827, PKS_AT, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit
SUPFAMiSSF47336, SSF47336, 1 hit
SSF52151, SSF52151, 1 hit
SSF53474, SSF53474, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit
TIGRFAMsiTIGR04532, PT_fungal_PKS, 1 hit
PROSITEiView protein in PROSITE
PS50075, CARRIER, 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 nameiAFLC_ASPPU
<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: Q12053
Secondary accession number(s): A0A0F0I481, Q6UEH2
<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: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 23, 2022
This is version 120 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

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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