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Entry version 57 (02 Jun 2021)
Sequence version 1 (13 Jun 2012)
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Protein

Fatty acid synthase subunit beta

Gene

FG00037

Organism
Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum)
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 subunit beta; part of the gene cluster that mediates the biosynthesis of gramillins A and B, bicyclic lipopeptides that induce cell death in maize leaves but not in wheat leaves (PubMed:30395461).

The nonribosomal peptide synthetase GRA1 incorporates respectively a glutamic adic (Glu), a leucine (Leu), a serine (Ser), a hydroxyglutamine (HOGln), a 2-amino decanoic acid, and 2 cysteins (CysB and CysA) (Probable). The biosynthesis of 2-amino decanoic acid incorporated in gramillins could be initiated by a fatty acid synthase composed of the alpha and beta subunits FGSG_00036 and FGSG_11656 (Probable). The cytochrome P450 monooxygenase FGSG_15680 could hydroxylate the fatty acid chain (Probable). Subsequent oxidation to the ketone by the oxidoreductase FGSG_00048 and transamination by aminotransferase FGSG_00049 could form 2-amino-decanoic acid (Probable). On the other hand, FGSG_15680 could also be responsible for the HO-modified glutamine at the gamma-position (Probable). Whether hydroxylation occurs on the fully assembled product or on the Gln residue prior to assembly into the gramillins requires further proof (Probable). The thioredoxin FGSG_00043 could also be required for the disulfide-bond formation between CysA and CysB (Probable). The specific involvement of the remaining proteins from the cluster is more difficult to discern, but could have broader regulatory (FGSG_00040 and FGSG_11657) or enzymatic functions (FGSG_00044 and FGSG_00045) (Probable). The final C-domain of GRA1 does not possess the expected sequence of a termination CT domain, often implicated in macrocyclization and release of a cyclopeptidein fungal NRPs; and the thioesterase FGSG_00047 may act in concert with the terminal C-domain of GRA1 to catalyze the formation of the macrocyclic anhydride and release of the products (Probable).

1 Publication1 Publication

<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 <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: Mycotoxin biosynthesis

This protein is involved in Mycotoxin biosynthesis.1 Publication
View all proteins of this organism that are known to be involved 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 sitei301For acetyltransferase activityUniRule annotation1
Active sitei1824For malonyltransferase activityUniRule annotation1

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

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

<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:
Fatty acid synthase subunit beta1 Publication (EC:2.3.1.861 Publication)
Alternative name(s):
S-acyl fatty acid synthase thioesteraseBy similarity (EC:3.1.2.14By similarity)
Including the following 3 domains:
3-hydroxyacyl-[acyl-carrier-protein] dehydrataseBy similarity (EC:4.2.1.59By similarity)
Enoyl-[acyl-carrier-protein] reductase [NADH]By similarity (EC:1.3.1.9By similarity)
[Acyl-carrier-protein] acetyltransferaseBy similarity (EC:2.3.1.38By similarity)
Alternative name(s):
Gramillins biosynthesis cluster protein FGSG_116561 Publication
[Acyl-carrier-protein] malonyltransferaseBy similarity (EC:2.3.1.39By similarity)
<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
ORF Names:FG00037, FGRAMPH1_01T00131, FGSG_11656
<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>OrganismiGibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum)
<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 identifieri229533 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusarium
<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
  • UP000070720 <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: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:FGRAMPH1_01G00131

<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_00004505621 – 2060Fatty acid synthase subunit betaAdd BLAST2060

<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 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%5Fsection">'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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
5518.FGSG_11656P0

<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

<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>Domaini1549 – 1661MaoC-likeSequence analysisAdd BLAST113

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 – 32DisorderedSequence analysisAdd BLAST32
Regioni182 – 543Acetyltransferase (AT) domainSequence analysisAdd BLAST362
Regioni600 – 845Enoyl reductase (ER) domainSequence analysisAdd BLAST246
Regioni1157 – 1640Dehydratase (DH) domainSequence analysisAdd BLAST484
Regioni1679 – 2043Malonyl/palmitoyl transferase (MT/PT) domainSequence analysisAdd BLAST365

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 biasi10 – 32Polar residuesSequence analysisAdd BLAST23

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QQJX, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000114_5_0_1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit
3.40.366.10, 3 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
IPR041099, FAS1_N
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
PF17828, FAS_N, 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%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.

I1S489-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFPGDMESKA SSMNGDQPSS PTPSSSTSVT IPTYTPTSMY DQELQFSRSV
60 70 80 90 100
AKHVYEAAAT LRAAFLCGFQ PYTDVASFAH DEIVSQLHYW SSFISFVNDP
110 120 130 140 150
ANNQAFTRMD ILEVTRALVQ CAEDTVLAGN DIHMIVAHLQ IPQSEKGRII
160 170 180 190 200
KTFVTANSML GDQPEVEVSN LVRSSLDGES TVYVIFGGQG NGDGYFAELA
210 220 230 240 250
ELYEVYQPLV GDLVRSASDL FRHLTDKMDV NDCFSEGMEL MAWIDKDNDT
260 270 280 290 300
PIPSRPYLLS SAISFPLITL LQLLHFKISF HYSGCSFKDV QRFLAGVTGH
310 320 330 340 350
SQGIIAAAAI AAVDSPASFH ELSLQAMTVS FSMGVRIHQY YGPQVLPQLI
360 370 380 390 400
TEACLAEGKP IPTPMLSVRG LSIETLATTI QDLNKSLPRT KVQLEVGLRN
410 420 430 440 450
NDSNYVITGD PMSLRGLCTH FDHKKKALDI VYQFLPAAAP YHNSYLSIAA
460 470 480 490 500
SRAIEDCQEI ILRGCDLKMP VFSTVDGSDL RNNEGANLVP DLIRMVCCQV
510 520 530 540 550
VNWPAALNMP GATHILDFGP GGAQGVGVLA NSMKAGQGVR VIHATVLNGL
560 570 580 590 600
NTELGYKPDL FDRSRKASER VSKPQPWVNS FQPTLTRFTE NKLVVSTRFT
610 620 630 640 650
RLFLQPPIMV AAMTPTTTSW DFVAAVMKAG FHAELACGGF HDRDSLSAAI
660 670 680 690 700
TAIANQVEPG TGITCNVIYS SPTSLRWQID ELEKLVAAGY QIDGLSIGAG
710 720 730 740 750
VPSVEVVQGY VERLQLQHIA LKPGSTEAIE RTLKIAKALQ PLPVVLQWTG
760 770 780 790 800
GRGGGHHSNQ DFHAPLISMY GKIRAQDNVV LVVGSGFGGP SDTLPYITGK
810 820 830 840 850
WASDMGLPPM PVDGILLGSR VMVAKEAHTS TEAKHLIVAT EGAPDDEWSG
860 870 880 890 900
TYSRPTGGVL SVISEMRQPI HKIATRAVRL WHELDQTIFH LGPKERVAEI
910 920 930 940 950
TRRRDEIIRR LNHDYHRVWF GCSGPTRDPV ELDEMTYSEV LHRFVELAYV
960 970 980 990 1000
TAEHRWVHLS WKKLFSELLT RTMSRLHRTS DSRSETLVDD LDDPYSTLAT
1010 1020 1030 1040 1050
LTDASAQLIT YEDSIYFLQL FRRRGQKPVP FIPVLDADFE TWFKKDSLWQ
1060 1070 1080 1090 1100
SEDIAAVPNH DAQRVCILHG PVAAQYSTKV DEPVGEILGN IHTAWVTAIL
1110 1120 1130 1140 1150
QTHYQGQSEL VPVFDNSPFH ASQVESSKTN TELSTPPLNH GLWTLEQWIV
1160 1170 1180 1190 1200
HIVQSRDKNL NWAKALLASP RVLCGRRLVP NPFITTLSGL RSMDIHVAET
1210 1220 1230 1240 1250
TKTGVGAGFT FFKIPLEETH QDLLDLTLQS NNEISIQISH YPTLQSAPIT
1260 1270 1280 1290 1300
LTHHMSCQFS KLAMNKSLSD RSAMIRDFYR RIWLGTSHES SHKSIYDKFE
1310 1320 1330 1340 1350
CEPYTVTADA IRKYNDCTRL PTSMPPTSWA TSEVPLDFAV VIAWKALVKP
1360 1370 1380 1390 1400
LFSRELEADI LKLLHVSNEI TLHSDHSPPM VHDVLHTESQ VTEVVLQPSG
1410 1420 1430 1440 1450
KMVQVEAHVF RGKSCILDLK TRFLLVGNDT HRDHLFRRSI LPPSEILLED
1460 1470 1480 1490 1500
EISAMQLVQS SWFQPLRDTS DLVGKRVVFQ LEDLMQFHEN GQIRCHQITG
1510 1520 1530 1540 1550
CAMLDGSIVG NCYLETPDDA YLSLMGNILS QQTGSSSQPA IFETPLLLFE
1560 1570 1580 1590 1600
EQEISFTAPT CEQTIAYSAA SGDSNPIHVS PVFASLAGLS SPIVHGMHIS
1610 1620 1630 1640 1650
AEVLQIVYTW LCASSMSRLK KSHVLFAGKV CTGDRLAVSM KHTAMHRGLR
1660 1670 1680 1690 1700
VVEVQIHKNM AEELVFVGTY EIEQPLTALV FTGQGSQKKG MGMDLRDKSA
1710 1720 1730 1740 1750
AARRIWDTAD DHFQHEYGFR ITDIVRHDPP SLTVHFGGVH GRRVRSNYMA
1760 1770 1780 1790 1800
LTYERVASDG QIIEAKLFPT INENTTKYVF SSESGLLSST QFTQPALGLM
1810 1820 1830 1840 1850
ELAIMADLEA RQLIPSNVTF AGHSLGEYSA LMAVGHIMPL EVFISTVFYR
1860 1870 1880 1890 1900
GLVMQSTVTY DHHGRSKYAM CAVDPTRVST DFDGQKLGWL VTQIASEGQW
1910 1920 1930 1940 1950
LLEVVNHNVI DSQYVCAGEA IALHCLGVVL DRIHYASKSF FDDGSFDLTD
1960 1970 1980 1990 2000
CIRESVKEIR KDRSKVVLSR SKASIPLKGL DVPFHSSHLR SGVDPFRRRL
2010 2020 2030 2040 2050
QRSIKLDNAS PTKLIGRYIP NLTGKPFEVT RQYFNEVLRL TGSIPIQQAL
2060
ESWDRVASTI
Length:2,060
Mass (Da):228,604
Last modified:June 13, 2012 - 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:iF24E6D1331407981
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
HG970332 Genomic DNA Translation: CEF71865.1

NCBI Reference Sequences

More...
RefSeqi
XP_011315624.1, XM_011317322.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
23558475

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
fgr:FGSG_11656

<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
HG970332 Genomic DNA Translation: CEF71865.1
RefSeqiXP_011315624.1, XM_011317322.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

STRINGi5518.FGSG_11656P0

Genome annotation databases

GeneIDi23558475
KEGGifgr:FGSG_11656

Organism-specific databases

VEuPathDBiFungiDB:FGRAMPH1_01G00131

Phylogenomic databases

eggNOGiENOG502QQJX, Eukaryota
HOGENOMiCLU_000114_5_0_1

Family and domain databases

Gene3Di3.20.20.70, 1 hit
3.40.366.10, 3 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
IPR041099, FAS1_N
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
PF17828, FAS_N, 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
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 nameiGRA7_GIBZE
<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: I1S489
Secondary accession number(s): A0A098D0C5
<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: August 12, 2020
Last sequence update: June 13, 2012
Last modified: June 2, 2021
This is version 57 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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