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Entry version 82 (10 Feb 2021)
Sequence version 1 (01 Jun 2002)
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Protein

Fatty acid synthase beta subunit aflB

Gene

aflB

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 transcript 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

Fatty acid synthase beta 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).

The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741, PubMed:15094053).

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, PubMed:8572694).

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 Publications17 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.

<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 functionHydrolase, Lyase, Multifunctional enzyme, Oxidoreductase, Transferase
LigandNAD, 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 beta subunit aflB1 Publication (EC:2.3.1.861 Publication)
Including the following 5 domains:
3-hydroxyacyl-[acyl-carrier-protein] dehydratase1 Publication (EC:4.2.1.591 Publication)
Enoyl-[acyl-carrier-protein] reductase [NADH]1 Publication (EC:1.3.1.91 Publication)
[Acyl-carrier-protein] acetyltransferase1 Publication (EC:2.3.1.381 Publication)
[Acyl-carrier-protein] malonyltransferase1 Publication (EC:2.3.1.391 Publication)
S-acyl fatty acid synthase thioesterase1 Publication (EC:3.1.2.141 Publication)
Alternative name(s):
Aflatoxin biosynthesis protein B1 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:aflB1 Publication
Synonyms:fas-11 Publication, fas-1A1 Publication, uvm81 Publication
ORF Names:P875_00052979
<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 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

Abolishes the production of norsolorinic acid and aflatoxin B1 (PubMed:8572694).1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004383371 – 1888Fatty acid synthase beta subunit aflBAdd BLAST1888

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q8TGA1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is regulated by the atfB, srrA, AP-1, and msnA transcription regulators (PubMed:23281343). These factors bind respectively to the conserved motifs CRE1 (5'-TGACATAA-3'), SRRA (5'-T/GNT/CAAGCCNNG/AA/GC/ANT/C-3'), AP-1 (5'-TGAGTAC-3') and STRE (5'-CCCCT-3'), present in the promoter of aflB (PubMed:23281343).1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<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
Q8TGA1

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>Domaini1399 – 1500MaoC-likeSequence analysisAdd BLAST102

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>Regioni23 – 395Acetyltransferase (AT) domainSequence analysis1 PublicationAdd BLAST373
Regioni437 – 682Enoyl reductase (ER) domainSequence analysis1 PublicationAdd BLAST246
Regioni990 – 1478Dehydratase (DH) domainSequence analysis1 PublicationAdd BLAST489
Regioni1517 – 1877Malonyl/palmitoyl transferase (MT/PT) domainSequence analysis1 PublicationAdd BLAST361

<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
3.20.20.70, 1 hit
3.40.366.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013785, Aldolase_TIM
IPR016452, Fas1/AflB-like
IPR013565, Fas1/AflB-like_central
IPR040883, FAS_meander
IPR003965, Fatty_acid_synthase
IPR029069, HotDog_dom_sf
IPR039569, MaoC-like_dehydrat_N
IPR002539, MaoC-like_dom
IPR032088, SAT

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF08354, DUF1729, 1 hit
PF17951, FAS_meander, 1 hit
PF13452, MaoC_dehydrat_N, 1 hit
PF01575, MaoC_dehydratas, 1 hit
PF16073, SAT, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005562, FAS_yeast_beta, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01483, FASYNTHASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00827, PKS_AT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52151, SSF52151, 2 hits
SSF54637, SSF54637, 2 hits

<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.

Q8TGA1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSVSREHES IPIQAAQRGA ARICAAFGGQ GSNNLDVLKG LLELYKRYGP
60 70 80 90 100
DLDELLDVAS NTLSQLASSP AAIDVHEPWG FDLRQWLTTP EVAPSKEILA
110 120 130 140 150
LPPRSFPLNT LLSLALYCAT CRELELDPGQ FRSLLHSSTG HSQGILAAVA
160 170 180 190 200
ITQAESWPTF YDACRTVLQI SFWIGLEAYL FTPSSAASDA MIQDCIEHGE
210 220 230 240 250
GLLSSMLSVS GLSRSQVERV IEHVNKGLGE CNRWVHLALV NSHEKFVLAG
260 270 280 290 300
PPQSLWAVCL HVRRIRADND LDQSRILFRN RKPIVDILFL PISAPFHTPY
310 320 330 340 350
LDGVQDRVIE ALSSASLALH SIKIPLYHTG TGSNLQELQP HQLIPTLIRA
360 370 380 390 400
ITVDQLDWPL VCRGLNATHV LDFGPGQTCS LIQELTQGTG VSVIQLTTQS
410 420 430 440 450
GPKPVGGHLA AVNWEAEFGL RLHANVHGAA KLHNRMTTLL GKPPVMVAGM
460 470 480 490 500
TPTTVRWDFV AAVAQAGYHV ELAGGGYHAE RQFEAEIRRL ATAIPADHGI
510 520 530 540 550
TCNLLYAKPT TFSWQISVIK DLVRQGVPVE GITIGAGIPS PEVVQECVQS
560 570 580 590 600
IGLKHISFKP GSFEAIHQVI QIARTHPNFL IGLQWTAGRG GGHHSWEDFH
610 620 630 640 650
GPILATYAQI RSCPNILLVV GSGFGGGPDT FPYLTGQWAQ AFGYPCMPFD
660 670 680 690 700
GVLLGSRMMV AREAHTSAQA KRLIIDAQGV GDADWHKSFD EPTGGVVTVN
710 720 730 740 750
SEFGQPIHVL ATRGVMLWKE LDNRVFSIKD TSKRLEYLRN HRQEIVSRLN
760 770 780 790 800
ADFARPWFAV DGHGQNVELE DMTYLEVLRR LCDLTYVSHQ KRWVDPSYRI
810 820 830 840 850
LLLDFVHLLR ERFQCAIDNP GEYPLDIIVR VEESLKDKAY RTLYPEDVSL
860 870 880 890 900
LMHLFSRRDI KPVPFIPRLD ERFETWFKKD SLWQSEDVEA VIGQDVQRIF
910 920 930 940 950
IIQGPMAVQY SISDDESVKD ILHNICNHYV EALQADSRET SIGDVHSITQ
960 970 980 990 1000
KPLSAFPGLK VTTNRVQGLY KFEKVGAVPE MDVLFEHIVG LSKSWARTCL
1010 1020 1030 1040 1050
MSKSVFRDGS RLHNPIRAAL QLQRGDTIEV LLTADSEIRK IRLISPTGDG
1060 1070 1080 1090 1100
GSTSKVVLEI VSNDGQRVFA TLAPNIPLSP EPSVVFCFKV DQKPNEWTLE
1110 1120 1130 1140 1150
EDASGRAERI KALYMSLWNL GFPNKASVLG LNSQFTGEEL MITTDKIRDF
1160 1170 1180 1190 1200
ERVLRQTSPL QLQSWNPQGC VPIDYCVVIA WSALTKPLMV SSLKCDLLDL
1210 1220 1230 1240 1250
LHSAISFHYA PSVKPLRVGD IVKTSSRILA VSVRPRGTML TVSADIQRQG
1260 1270 1280 1290 1300
QHVVTVKSDF FLGGPVLACE TPFELTEEPE MVVHVDSEVR RAILHSRKWL
1310 1320 1330 1340 1350
MREDRALDLL GRQLLFRLKS EKLFRPDGQL ALLQVTGSVF SYSPDGSTTA
1360 1370 1380 1390 1400
FGRVYFESES CTGNVVMDFL HRYGAPRAQL LELQHPGWTG TSTVAVRGPR
1410 1420 1430 1440 1450
RSQSYARVSL DHNPIHVCPA FARYAGLSGP IVHGMETSAM MRRIAEWAIG
1460 1470 1480 1490 1500
DADRSRFRSW HITLQAPVHP NDPLRVELQH KAMEDGEMVL KVQAFNERTE
1510 1520 1530 1540 1550
ERVAEADAHV EQETTAYVFC GQGSQRQGMG MDLYVNCPEA KALWARADKH
1560 1570 1580 1590 1600
LWEKYGFSIL HIVQNNPPAL TVHFGSQRGR RIRANYLRMM GQPPIDGRHP
1610 1620 1630 1640 1650
PILKGLTRNS TSYTFSYSQG LLMSTQFAQP ALALMEMAQF EWLKAQGVVQ
1660 1670 1680 1690 1700
KGARFAGHSL GEYAALGACA SFLSFEDLIS LIFYRGLKMQ NALPRDANGH
1710 1720 1730 1740 1750
TDYGMLAADP SRIGKGFEEA SLKCLVHIIQ QETGWFVEVV NYNINSQQYV
1760 1770 1780 1790 1800
CAGHFRALWM LGKICDDLSC HPQPETVEGQ ELRAMVWKHV PTVEQVPRED
1810 1820 1830 1840 1850
RMERGRATIP LPGIDIPYHS TMLRGEIEPY REYLSERIKV GDVKPCELVG
1860 1870 1880
RWIPNVVGQP FSVDKSYVQL VHGITGSPRL HSLLQQMA
Length:1,888
Mass (Da):210,430
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:iEC232BC88FA5F05C
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 KJK60796 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF391094 Genomic DNA Translation: AAL99899.1
AY371490 Genomic DNA Translation: AAS66003.1
JZEE01000728 Genomic DNA Translation: KJK60796.1 Sequence problems.

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
KJK60796; KJK60796; P875_00052979

<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: AAL99899.1
AY371490 Genomic DNA Translation: AAS66003.1
JZEE01000728 Genomic DNA Translation: KJK60796.1 Sequence problems.

3D structure databases

SMRiQ8TGA1
ModBaseiSearch...

Proteomic databases

PRIDEiQ8TGA1

Genome annotation databases

EnsemblFungiiKJK60796; KJK60796; P875_00052979

Enzyme and pathway databases

UniPathwayiUPA00287

Family and domain databases

Gene3Di3.20.20.70, 1 hit
3.40.366.10, 2 hits
InterProiView protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013785, Aldolase_TIM
IPR016452, Fas1/AflB-like
IPR013565, Fas1/AflB-like_central
IPR040883, FAS_meander
IPR003965, Fatty_acid_synthase
IPR029069, HotDog_dom_sf
IPR039569, MaoC-like_dehydrat_N
IPR002539, MaoC-like_dom
IPR032088, SAT
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF08354, DUF1729, 1 hit
PF17951, FAS_meander, 1 hit
PF13452, MaoC_dehydrat_N, 1 hit
PF01575, MaoC_dehydratas, 1 hit
PF16073, SAT, 1 hit
PIRSFiPIRSF005562, FAS_yeast_beta, 1 hit
PRINTSiPR01483, FASYNTHASE
SMARTiView protein in SMART
SM00827, PKS_AT, 1 hit
SUPFAMiSSF52151, SSF52151, 2 hits
SSF54637, SSF54637, 2 hits

MobiDB: a database of protein disorder and mobility annotations

More...
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 nameiAFLB_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: Q8TGA1
Secondary accession number(s): A0A0F0I0T2
<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: February 10, 2021
This is version 82 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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