Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 cytodhrome 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_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pantetheine 4'-phosphate1 PublicationNote: Binds 1 phosphopantetheine covalently.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: 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 ‘Function’ 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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Multifunctional enzyme, Transferase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-17895

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_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:
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_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:aflC1 Publication
Synonyms:pksA1 Publication, pksL11 Publication
ORF Names:P875_00052995
<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 parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)
<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 identifieri1403190 [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
  • UP000033540 <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

<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_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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.<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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q12053

<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_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-15811477,EBI-15811477

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-59286N

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q12053

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

More...
SMRi
Q12053

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_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>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
Regioni1867 – 2102Thioesterase/Claisen cyclase (TE/CLC) domainSequence analysisAdd BLAST236

<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
3.40.366.10, 1 hit
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
IPR032821 KAsynt_C_assoc
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR016036 Malonyl_transacylase_ACP-bd
IPR020801 PKS_acyl_transferase
IPR020841 PKS_Beta-ketoAc_synthase_dom
IPR020807 PKS_dehydratase
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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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.

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[»]
ProteinModelPortaliQ12053
SMRiQ12053
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59286N

Protein family/group databases

ESTHERiaspor-PKSL1 Thioesterase

Proteomic databases

PRIDEiQ12053

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiKJK60793; KJK60793; P875_00052995

Enzyme and pathway databases

UniPathwayi
UPA00287

BioCyciMetaCyc:MONOMER-17895
BRENDAi2.3.1.221 523

Miscellaneous databases

EvolutionaryTraceiQ12053

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.40.366.10, 1 hit
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
IPR032821 KAsynt_C_assoc
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR016036 Malonyl_transacylase_ACP-bd
IPR020801 PKS_acyl_transferase
IPR020841 PKS_Beta-ketoAc_synthase_dom
IPR020807 PKS_dehydratase
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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_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 1, 1997
Last sequence update: November 1, 1997
Last modified: December 5, 2018
This is version 108 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again