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Entry version 115 (29 Sep 2021)
Sequence version 1 (01 Jun 2002)
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Protein

Fatty acid synthase alpha subunit aflA

Gene

aflA

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>
-Protein inferred from homologyi <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

Fatty acid synthase alpha subunit; 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:15006741, PubMed:15094053).

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: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 Publications16 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: aflatoxin biosynthesis

This protein is involved in the pathway aflatoxin biosynthesis, which is part of Mycotoxin biosynthesis.3 Publications
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_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 sitei1113For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1552MagnesiumBy similarity1
Metal bindingi1653MagnesiumBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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 functionMultifunctional enzyme, Oxidoreductase, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandMagnesium, Metal-binding, NADP

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00287

<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:
Fatty acid synthase alpha subunit aflA1 Publication (EC:2.3.1.861 Publication)
Including the following 2 domains:
3-oxoacyl-[acyl-carrier-protein] reductase1 Publication (EC:1.1.1.1001 Publication)
Alternative name(s):
Beta-ketoacyl reductaseCurated
3-oxoacyl-[acyl-carrier-protein] synthase1 Publication (EC:2.3.1.411 Publication)
Alternative name(s):
Aflatoxin biosynthesis protein 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:aflA1 Publication
Synonyms:fas-21 Publication, fas-2A, hexA1 Publication
ORF Names:P875_00052994
<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 location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<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_00004383361 – 1671Fatty acid synthase alpha subunit aflAAdd BLAST1671

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 residuei113O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

4'-phosphopantetheine is transferred from CoA to a specific serine of the acyl carrier domain by the C-terminal PPT domain. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q8TGA2

<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">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).

By similarity

<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
Q8TGA2

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>Domaini75 – 153CarrierPROSITE-ProRule annotation1 PublicationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni40 – 60DisorderedSequence analysisAdd BLAST21
Regioni492 – 729Ketoreductase (KR) domainSequence analysis1 PublicationAdd BLAST238
Regioni833 – 1417Ketosynthase (KS) domainSequence analysis1 PublicationAdd BLAST585
Regioni1244 – 1288DisorderedSequence analysisAdd BLAST45
Regioni1497 – 1521DisorderedSequence analysisAdd BLAST25
Regioni1552 – 1554Acetyl-CoA bindingBy similarity3
Regioni1598 – 1614Acetyl-CoA bindingBy similarityAdd BLAST17
Regioni1622 – 1625Acetyl-CoA bindingBy similarity4
Regioni1652 – 1654Acetyl-CoA bindingBy similarity3

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 biasi1244 – 1283Polar residuesSequence analysisAdd BLAST40

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.470.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008278, 4-PPantetheinyl_Trfase_dom
IPR037143, 4-PPantetheinyl_Trfase_dom_sf
IPR040899, Fas_alpha_ACP
IPR026025, FAS_alpha_yeast
IPR041550, FASI_helical
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR036291, NAD(P)-bd_dom_sf
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR013968, PKS_KR
IPR009081, PP-bd_ACP
IPR004568, Ppantetheine-prot_Trfase_dom
IPR016039, Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01648, ACPS, 1 hit
PF18325, Fas_alpha_ACP, 1 hit
PF18314, FAS_I_H, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000454, FAS_yeast_alpha, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00825, PKS_KS, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735, SSF51735, 1 hit
SSF53901, SSF53901, 2 hits
SSF56214, SSF56214, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00556, pantethn_trn, 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.

Q8TGA2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVIQGKRLAA SSIQLLASSL DAKKLCYEYD ERQAPGVTQI TEEAPTEQPP
60 70 80 90 100
LSTPPSLPQT PNISPISASK IVIDDVALSR VQIVQALVAR KLKTAIAQLP
110 120 130 140 150
TSKSIKELSG GRSSLQNELV GDIHNEFSSI PDAPEQILLR DFGDANPTVQ
160 170 180 190 200
LGKTSSAAVA KLISSKMPSD FNANAIRAHL ANKWGLGPLR QTAVLLYAIA
210 220 230 240 250
SEPPSRLASS SAAEEYWDNV SSMYAESCGI TLRPRQDTMN EDAMASSAID
260 270 280 290 300
PAVVAEFSKG HRRLGVQQFQ ALAEYLQIDL SGSQASQSDA LVAELQQKVD
310 320 330 340 350
LWTAEMTPEF LAGISPMLDV KKSRRYGSWW NMARQDVLAF YRRPSYSEFV
360 370 380 390 400
DDALAFKVFL NRLCNRADEA LLNMVRSLSC DAYFKQGSLP GYHAASRLLE
410 420 430 440 450
QAITSTVADC PKARLILPAV GPHTTITKDG TIEYAEAPRQ GVSGPTAYIQ
460 470 480 490 500
SLRQGASFIG LKSADVDTQS NLTDALLDAM CLALHNGISF VGKTFLVTGA
510 520 530 540 550
GQGSIGAGVV RLLLEGGARV LVTTSREPAT TSRYFQQMYD NHGAKFSELR
560 570 580 590 600
VVPCNLASAQ DCEGLIRHVY DPRGLNWDLD AILPFAAASD YSTEMHDIRG
610 620 630 640 650
QSELGHRLML VNVFRVLGHI VHCKRDAGVD CHPTQVLLPL SPNHGIFGGD
660 670 680 690 700
GMYPESKLAL ESLFHRIRSE SWSDQLSICG VRIGWTRSTG LMTAHDIIAE
710 720 730 740 750
TVEEHGIRTF SVAEMALNIA MLLTPDFVAH CEDGPLDADF TGSLGTLGSI
760 770 780 790 800
PGFLAQLHQK VQLAAEVIRA VQAEDEHERF LSPGTKPTLQ APVAPMHPRS
810 820 830 840 850
SLRVGYPRLP DYEQEIRPLS PRLERLQDPA NAVVVVGYSE LGPWGSARLR
860 870 880 890 900
WEIESQGQWT SAGYVELAWL MNLIRHVNDE SYVGWVDTQT GKPVRDGEIQ
910 920 930 940 950
ALYGDHIDNH TGIRPIQSTS YNPERMEVLQ EVAVEEDLPE FEVSQLTADA
960 970 980 990 1000
MRLRHGANVS IRPSGNPDAC HVKLKRGAVI LVPKTVPFVW GSCAGELPKG
1010 1020 1030 1040 1050
WTPAKYGIPE NLIHQVDPVT LYTICCVAEA FYSAGITHPL EVFRHIHLSE
1060 1070 1080 1090 1100
LGNFIGSSMG GPTKTRQLYR DVYFDHEIPS DVLQDTYLNT PAAWVNMLLL
1110 1120 1130 1140 1150
GCTGPIKTPV GACATGVESI DSGYESIMAG KTKMCLVGGY DDLQEEASYG
1160 1170 1180 1190 1200
FAQLKATVNV EEEIACGRQP SEMSRPMAES RAGFVEAHGC GVQLLCRGDI
1210 1220 1230 1240 1250
ALQMGLPIYA VIASSAMAAD KIGSSVPAPG QGILSFSRER ARSSMISVTS
1260 1270 1280 1290 1300
RPSSRSSTSS EVSDKSSLTS ITSISNPAPR AQRARSTTDM APLRAALATW
1310 1320 1330 1340 1350
GLTIDDLDVA SLHGTSTRGN DLNEPEVIET QMRHLGRTPG RPLWAICQKS
1360 1370 1380 1390 1400
VTGHPKAPAA AWMLNGCLQV LDSGLVPGNR NLDTLDEALR SASHLCFPTR
1410 1420 1430 1440 1450
TVQLREVKAF LLTSFGFGQK GGQVVGVAPK YFFATLPRPE VEGYYRKVRV
1460 1470 1480 1490 1500
RTEAGDRAYA AAVMSQAVVK IQTQNPYDEP DAPRIFLDPL ARISQDPSTG
1510 1520 1530 1540 1550
QYRFRSDATP ALDDDALPPP GEPTELVKGI SSAWIEEKVR PHMSPGGTVG
1560 1570 1580 1590 1600
VDLVPLASFD AYKNAIFVER NYTVRERDWA EKSADVRAAY ASRWCAKEAV
1610 1620 1630 1640 1650
FKCLQTHSQG AGAAMKEIEI EHGGNGAPKV KLRGAAQTAA RQRGLEGVQL
1660 1670
SISYGDDAVI AVALGLMSGA S
Length:1,671
Mass (Da):181,275
Last modified:June 1, 2002 - 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:i266034C51A556FFE
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence KJK60794 differs from that shown. Reason: Erroneous gene model prediction.Curated

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
AF391094 Genomic DNA Translation: AAL99898.1
AY371490 Genomic DNA Translation: AAS66002.1
JZEE01000728 Genomic DNA Translation: KJK60794.1 Sequence problems.

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
KJK60794; KJK60794; P875_00052994

<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
AF391094 Genomic DNA Translation: AAL99898.1
AY371490 Genomic DNA Translation: AAS66002.1
JZEE01000728 Genomic DNA Translation: KJK60794.1 Sequence problems.

3D structure databases

SMRiQ8TGA2
ModBaseiSearch...

Proteomic databases

PRIDEiQ8TGA2

Genome annotation databases

EnsemblFungiiKJK60794; KJK60794; P875_00052994

Enzyme and pathway databases

UniPathwayiUPA00287

Family and domain databases

Gene3Di3.90.470.20, 1 hit
InterProiView protein in InterPro
IPR008278, 4-PPantetheinyl_Trfase_dom
IPR037143, 4-PPantetheinyl_Trfase_dom_sf
IPR040899, Fas_alpha_ACP
IPR026025, FAS_alpha_yeast
IPR041550, FASI_helical
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR036291, NAD(P)-bd_dom_sf
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR013968, PKS_KR
IPR009081, PP-bd_ACP
IPR004568, Ppantetheine-prot_Trfase_dom
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF01648, ACPS, 1 hit
PF18325, Fas_alpha_ACP, 1 hit
PF18314, FAS_I_H, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PIRSFiPIRSF000454, FAS_yeast_alpha, 1 hit
SMARTiView protein in SMART
SM00825, PKS_KS, 1 hit
SUPFAMiSSF51735, SSF51735, 1 hit
SSF53901, SSF53901, 2 hits
SSF56214, SSF56214, 1 hit
TIGRFAMsiTIGR00556, pantethn_trn, 1 hit
PROSITEiView protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiAFLA_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: Q8TGA2
Secondary accession number(s): A0A0F0HZ47
<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 30, 2016
Last sequence update: June 1, 2002
Last modified: September 29, 2021
This is version 115 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
  2. SIMILARITY comments
    Index of protein domains and families
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