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Protein

Fatty acid synthase subunit beta

Gene

FAS1

Organism
Candida albicans (Yeast)
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 synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.

<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

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 sitei261For acetyltransferase activityBy similarity1
Active sitei1796For malonyltransferase activityBy 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 functionHydrolase, Lyase, Multifunctional enzyme, Oxidoreductase, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
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_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 subunit beta (EC:2.3.1.86)
Including the following 5 domains:
3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.59)
Enoyl-[acyl-carrier-protein] reductase [NADH] (EC:1.3.1.9)
[Acyl-carrier-protein] acetyltransferase (EC:2.3.1.38)
[Acyl-carrier-protein] malonyltransferase (EC:2.3.1.39)
S-acyl fatty acid synthase thioesterase (EC:3.1.2.14)
<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:FAS1
<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>OrganismiCandida albicans (Yeast)
<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 identifieri5476 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

<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_00001802801 – 2037Fatty acid synthase subunit betaAdd BLAST2037

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P34731

<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).

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P34731

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

More...
SMRi
P34731

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Domaini1506 – 1634MaoC-likeAdd BLAST129

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 – 453AcetyltransferaseBy similarityAdd BLAST453
Regioni465 – 798Enoyl reductaseBy similarityAdd BLAST334
Regioni1132 – 1612DehydrataseBy similarityAdd BLAST481
Regioni1613 – 1833Malonyl/palmitoyl transferaseBy similarityAdd BLAST221

<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, 2 hits
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
IPR013565 DUF1729
IPR003965 Fatty_acid_synthase
IPR016452 Fatty_acid_Synthase_bsu_fun
IPR029069 HotDog_dom_sf
IPR039569 MaoC-like_dehydrat_N
IPR002539 MaoC-like_dom
IPR020801 PKS_acyl_transferase
IPR032088 SAT

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698 Acyl_transf_1, 1 hit
PF08354 DUF1729, 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>.<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.

P34731-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTHRPFQLT HGSIEHTLLV PNDLFFNYSQ LKDEFIKTLP EPTEGFAGDD
60 70 80 90 100
EPSSPAELYG KFIGFISNAQ FPQIVELSLK DFESRFLDNN NDNIHSFAVK
110 120 130 140 150
LLDDETYPTT IAKVKENIVK NYYKAVKSIN KVESNLLYHC KHDAKLVAIF
160 170 180 190 200
GGQGNTDDYF EELRELYTLY QGLIEDLLVS IAEKLNQLHP SFDKIYTQGL
210 220 230 240 250
NILSWLKHPE TTPDQDYLLS VPVSCPVICV IQLCHYTITC KVLGLTPGEF
260 270 280 290 300
RNSLKWSTGH SQGLVTAVTI AASDSWDSFL KNSLTAVSLL LFIGSRCLST
310 320 330 340 350
YPRTSLPPTM LQDSLDNGEG RPSPMLSVRD LSIKQVEKFI EQTNSHLPRE
360 370 380 390 400
KHIAISLING ARNLVLSGPP ESLYGFNLNL RNQKAPMGLD QSRVPFSERK
410 420 430 440 450
LKCSNRFLPI FAPFHSHLLA DATELILDDV KEHGLSFEGL KIPVYDTFDG
460 470 480 490 500
SDFQALKEPI IDRVVKLITE LPVHWEEATN HKATHILDFG PGGVSGLGVL
510 520 530 540 550
THRNKEGTGA RIILAGTLDS NPIDDEYGFK HEIFQTSADK AIKWAPDWLK
560 570 580 590 600
ELRPTLVKNS EGKIYVKTKF SQLLGRAPLM VAGMTPTTVN TDIVSASLNA
610 620 630 640 650
GYHIELAGGG YFSPVMMTRA IDDIVSRIKP GYGLGINLIY VNPFMLQWGI
660 670 680 690 700
PLIKDLREKG YPIQSLTIGA GVPSIEVATE YIEDLGLTHL GLKPGSVDAI
710 720 730 740 750
SQVIAIAKAH PTFPIVLQWT GGRGGGHHSF EDFHQPIIQM YSKIRRCSNI
760 770 780 790 800
VLVAGSGFGS DEDTYPYLSG YWSEKFNYPP MPFDGVLFGS RVMTSKESHT
810 820 830 840 850
SLAAKKLIVE CKGVPDQQWE QTYKKPTGGI ITVRSEMGEP IHKIATRGVM
860 870 880 890 900
FWKELDDTIF NLPKNKLLDA LNKKRDHIIK KLNNDFQKPW FGKNANGVCD
910 920 930 940 950
LQEMTYKEVA NRLVELMYVK KSHRWIDVSL RNMYGDFLRR VEERFTSSAG
960 970 980 990 1000
TVSLLQNFNQ LNEPEQFTAD FFEKFPQAGK QLISEEDCDY FLMLAARPGQ
1010 1020 1030 1040 1050
KPVPFVPVLD ERFEFFFKKD SLWQSEDLES VVDEDVQRTC ILHGPVASQY
1060 1070 1080 1090 1100
TSKVDEPIGD ILNSIHEGHI ARLIKEEYAG DESKIPVVEY FGGKKPASVS
1110 1120 1130 1140 1150
ATSVNIIDGN QVVYEIDSEL PNKQEWLDLL AGTELNWLQA FISTDRIVQG
1160 1170 1180 1190 1200
SKHVSNPLHD ILTPAKHSKV TIDKKTKKLT AFENIKGDLL PVVEIELVKP
1210 1220 1230 1240 1250
NTIQLSLIEH RTADTNPVAL PFLYKYNPAD GFAPILEIME DRNERIKEFY
1260 1270 1280 1290 1300
WKLWFGSSVP YSNDINVEKA ILGDEITISS QTISEFTHAI GNKCDAFVDR
1310 1320 1330 1340 1350
PGKATLAPMD FAIVIGWKAI IKAIFPKSVD GDLLKLVHLS NGYKMITGAA
1360 1370 1380 1390 1400
PLKKGDVVST KAEIKAVLNQ PSGKLVEVVG TIYREGKPVM EVTSQFLYRG
1410 1420 1430 1440 1450
EYNDYCNTFQ KVTETPVQVA FKSAKDLAVL RSKEWFHLEK DVQFDVLTFR
1460 1470 1480 1490 1500
CESTYKFKSA NVYSSIKTTG QVLLELPTKE VIQVGSVDYE AGTSYGNPVT
1510 1520 1530 1540 1550
DYLSRNGKTI EESVIFENAI PLSSGEELTS KAPGTNEPYA IVSGDYNPIH
1560 1570 1580 1590 1600
VSRVFAAYAK LPGTITHGMY SSASIRALVE EWAANNVAAR VRAFKCDFVG
1610 1620 1630 1640 1650
MVLPNDTLQT TMEHVGMING RKIIKVETRN VETELPVLIG EAEIEQPTTT
1660 1670 1680 1690 1700
YVFTGQGSQE QGMGMELYNS SEVAREVWDK ADRHFVNNYG FSILDIVQNN
1710 1720 1730 1740 1750
PNELTIHFGG AKGRAIRDNY IGMMFETIGE DGALKSEKIF KDIDETTTSY
1760 1770 1780 1790 1800
TFVSPTGLLS ATQFTQPALT LMEKAAYEDI KSKGLIPSDI MFAGHSLGEY
1810 1820 1830 1840 1850
SALSSLANVM PIESLVDVVF YRGMTMQVAV PRDELGRSNY GMVAVNPSRV
1860 1870 1880 1890 1900
SATFDDSALR FVVDEVANKT KWLLEIVNYN VENQQYVAAG DLRALDTLTN
1910 1920 1930 1940 1950
VLNVLKINKI DIVKLQEQMS IEKVKEHLYE IVDEVAAKSL AKPQPIDLER
1960 1970 1980 1990 2000
GFAVIPLKGI SVPFHSSYLM SGVKPFQRFL CKKIPKSSVK PQDLIGKYIP
2010 2020 2030
NLTAKPFELT KEYFQSVYDL TKSEKIKSIL DNWEQYE
Length:2,037
Mass (Da):227,919
Last modified:February 1, 1994 - 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:iD37BDD0DB9A8ADDA
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X74952 Genomic DNA Translation: CAA52907.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S37178

<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
X74952 Genomic DNA Translation: CAA52907.1
PIRiS37178

3D structure databases

ProteinModelPortaliP34731
SMRiP34731
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP34731

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.20.20.70, 2 hits
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
IPR013565 DUF1729
IPR003965 Fatty_acid_synthase
IPR016452 Fatty_acid_Synthase_bsu_fun
IPR029069 HotDog_dom_sf
IPR039569 MaoC-like_dehydrat_N
IPR002539 MaoC-like_dom
IPR020801 PKS_acyl_transferase
IPR032088 SAT
PfamiView protein in Pfam
PF00698 Acyl_transf_1, 1 hit
PF08354 DUF1729, 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

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 nameiFAS1_CANAX
<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: P34731
<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: February 1, 1994
Last sequence update: February 1, 1994
Last modified: December 5, 2018
This is version 101 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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