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Q9UUG0 (FAS1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid synthase subunit beta

EC=2.3.1.86

Including the following 5 domains:

  1. 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
    EC=4.2.1.59
  2. Enoyl-[acyl-carrier-protein] reductase [NADH]
    EC=1.3.1.9
  3. [Acyl-carrier-protein] acetyltransferase
    EC=2.3.1.38
  4. [Acyl-carrier-protein] malonyltransferase
    EC=2.3.1.39
  5. S-acyl fatty acid synthase thioesterase
    EC=3.1.2.14
Gene names
Name:fas1
ORF Names:SPAC926.09c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length2073 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+.

Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].

Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein].

A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.

Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.

Subunit structure

[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta). Ref.1

Sequence similarities

Belongs to the fungal fatty acid synthetase subunit beta family.

Contains 1 MaoC-like domain.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   LigandNAD
NADP
   Molecular functionHydrolase
Lyase
Oxidoreductase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from direct assay Ref.1. Source: PomBase

   Cellular_componentcytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

fatty acid synthase complex

Inferred from direct assay Ref.1. Source: PomBase

   Molecular_function3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity

Inferred from sequence orthology. Source: PomBase

[acyl-carrier-protein] S-acetyltransferase activity

Inferred from sequence orthology. Source: PomBase

[acyl-carrier-protein] S-malonyltransferase activity

Inferred from sequence orthology. Source: PomBase

enoyl-[acyl-carrier-protein] reductase (NADH) activity

Inferred from sequence orthology. Source: PomBase

fatty acid synthase activity

Inferred from direct assay Ref.1. Source: PomBase

fatty-acyl-CoA synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

myristoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

oleoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

palmitoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20732073Fatty acid synthase subunit beta
PRO_0000180281

Regions

Domain1558 – 1667110MaoC-like
Region1 – 459459Acetyltransferase
Region470 – 858389Enoyl reductase
Region1155 – 1644490Dehydratase
Region1645 – 2073429Malonyl/palmitoyl transferase

Sites

Active site2701For acetyltransferase activity By similarity
Active site13611For dehydratase activity Potential
Active site18281For malonyltransferase activity By similarity

Amino acid modifications

Modified residue11221Phosphoserine Ref.4
Modified residue20731Phosphoserine Ref.4

Experimental info

Sequence conflict2221P → R in BAA36384. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9UUG0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D928270838E7C7C4

FASTA2,073230,561
        10         20         30         40         50         60 
MVEAEQVHQS LRSLVLSYAH FSPSILIPAS QYLLAAQLRD EFLSLHPAPS AESVEKEGAE 

        70         80         90        100        110        120 
LEFEHELHLL AGFLGLIAAK EEETPGQYTQ LLRIITLEFE RTFLAGNEVH AVVHSLGLNI 

       130        140        150        160        170        180 
PAQKDVVRFY YHSCALIGQT TKFHGSALLD ESSVKLAAIF GGQGYEDYFD ELIELYEVYA 

       190        200        210        220        230        240 
PFAAELIQVL SKHLFTLSQN EQASKVYSKG LNVLDWLAGE RPERDYLVSA PVSLPLVGLT 

       250        260        270        280        290        300 
QLVHFSVTAQ ILGLNPGELA SRFSAASGHS QGIVVAAAVS ASTDSASFME NAKVALTTLF 

       310        320        330        340        350        360 
WIGVRSQQTF PTTTLPPSVV ADSLASSEGN PTPMLAVRDL PIETLNKHIE TTNTHLPEDR 

       370        380        390        400        410        420 
KVSLSLVNGP RSFVVSGPAR SLYGLNLSLR KEKADGQNQS RIPHSKRKLR FINRFLSISV 

       430        440        450        460        470        480 
PFHSPYLAPV RSLLEKDLQG LQFSALKVPV YSTDDAGDLR FEQPSKLLLA LAVMITEKVV 

       490        500        510        520        530        540 
HWEEACGFPD VTHIIDFGPG GISGVGSLTR ANKDGQGVRV IVADSFESLD MGAKFEIFDR 

       550        560        570        580        590        600 
DAKSIEFAPN WVKLYSPKLV KNKLGRVYVD TRLSRMLGLP PLWVAGMTPT SVPWQFCSAI 

       610        620        630        640        650        660 
AKAGFTYELA GGGYFDPKMM REAIHKLSLN IPPGAGICVN VIYINPRTYA WQIPLIRDMV 

       670        680        690        700        710        720 
AEGYPIRGVT IAAGIPSLEV ANELISTLGV QYLCLKPGSV EAVNAVISIA KANPTFPIVL 

       730        740        750        760        770        780 
QWTGGRAGGH HSFEDFHSPI LLTYSAIRRC DNIVLIAGSG FGGADDTEPY LTGEWSAAFK 

       790        800        810        820        830        840 
LPPMPFDGIL FGSRLMVAKE AHTSLAAKEA IVAAKGVDDS EWEKTYDGPT GGIVTVLSEL 

       850        860        870        880        890        900 
GEPIHKLATR GIMFWKELDD TIFSLPRPKR LPALLAKKQY IIKRLNDDFQ KVYFPAHIVE 

       910        920        930        940        950        960 
QVSPEKFKFE AVDSVEDMTY AELLYRAIDL MYVTKEKRWI DVTLRTFTGK LMRRIEERFT 

       970        980        990       1000       1010       1020 
QDVGKTTLIE NFEDLNDPYP VAARFLDAYP EASTQDLNTQ DAQFFYSLCS NPFQKPVPFI 

      1030       1040       1050       1060       1070       1080 
PAIDDTFEFY FKKDSLWQSE DLAAVVGEDV GRVAILQGPM AAKHSTKVNE PAKELLDGIN 

      1090       1100       1110       1120       1130       1140 
ETHIQHFIKK FYAGDEKKIP IVEYFGGVPP VNVSHKSLES VSVTEEAGSK VYKLPEIGSN 

      1150       1160       1170       1180       1190       1200 
SALPSKKLWF ELLAGPEYTW FRAIFTTQRV AKGWKLEHNP VRRIFAPRYG QRAVVKGKDN 

      1210       1220       1230       1240       1250       1260 
DTVVELYETQ SGNYVLAARL SYDGETIVVS MFENRNALKK EVHLDFLFKY EPSAGYSPVS 

      1270       1280       1290       1300       1310       1320 
EILDGRNDRI KHFYWALWFG EEPYPENASI TDTFTGPEVT VTGNMIEDFC RTVGNHNEAY 

      1330       1340       1350       1360       1370       1380 
TKRAIRKRMA PMDFAIVVGW QAITKAIFPK AIDGDLLRLV HLSNSFRMVG SHSLMEGDKV 

      1390       1400       1410       1420       1430       1440 
TTSASIIAIL NNDSGKTVTV KGTVYRDGKE VIEVISRFLY RGTFTDFENT FEHTQETPMQ 

      1450       1460       1470       1480       1490       1500 
LTLATPKDVA VLQSKSWFQL LDPSQDLSGS ILTFRLNSYV RFKDQKVKSS VETKGIVLSE 

      1510       1520       1530       1540       1550       1560 
LPSKAIIQVA SVDFQSVDCH GNPVIEFLKR NGKPIEQPVE FENGGYSVIQ VMDEGYSPVF 

      1570       1580       1590       1600       1610       1620 
VTPPTNSPYA EVSGDYNPIH VSPTFAAFVE LPGTHGITHG MYTSAAARRF VETYAAQNVP 

      1630       1640       1650       1660       1670       1680 
ERVKHYEVTF VNMVLPNTEL ITKLSHTGMI NGRKIIKVEV LNQETSEPVL VGTAEVEQPV 

      1690       1700       1710       1720       1730       1740 
SAYVFTGQGS QEQGMGMDLY ASSPVARKIW DSADKHFLTN YGFSIIDIVK HNPHSITIHF 

      1750       1760       1770       1780       1790       1800 
GGSKGKKIRD NYMAMAYEKL MEDGTSKVVP VFETITKDST SFSFTHPSGL LSATQFTQPA 

      1810       1820       1830       1840       1850       1860 
LTLMEKSAFE DMRSKGLVQN DCAFAGHSLG EYSALSAMGD VLSIEALVDL VFLRGLTMQN 

      1870       1880       1890       1900       1910       1920 
AVHRDELGRS DYGMVAANPS RVSASFTDAA LRFIVDHIGQ QTNLLLEIVN YNVENQQYVV 

      1930       1940       1950       1960       1970       1980 
SGNLLSLSTL GHVLNFLKVQ KIDFEKLKET LTIEQLKEQL TDIVEACHAK TLEQQKKTGR 

      1990       2000       2010       2020       2030       2040 
IELERGYATI PLKIDVPFHS SFLRGGVRMF REYLVKKIFP HQINVAKLRG KYIPNLTAKP 

      2050       2060       2070 
FEISKEYFQN VYDLTGSQRI KKILQNWDEY ESS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the fatty acid synthetase beta subunit from fission yeast, coexpression with the alpha subunit, and purification of the intact multifunctional enzyme complex."
Niwa H., Katayama E., Yanagida M., Morikawa K.
Protein Expr. Purif. 13:403-413(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1725-2073.
Strain: PR745.
[4]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1122 AND SER-2073, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB010274 Genomic DNA. Translation: BAA36384.1.
CU329670 Genomic DNA. Translation: CAB54157.1.
D89148 mRNA. Translation: BAA13810.1.
PIRT39207.
T42424.
T43311.
RefSeqNP_594370.1. NM_001019791.2.

3D structure databases

ProteinModelPortalQ9UUG0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279916. 17 interactions.
MINTMINT-4713190.
STRING4896.SPAC926.09c-1.

Proteomic databases

PaxDbQ9UUG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC926.09c.1; SPAC926.09c.1:pep; SPAC926.09c.
GeneID2543497.
KEGGspo:SPAC926.09c.

Organism-specific databases

PomBaseSPAC926.09c.

Phylogenomic databases

eggNOGCOG0331.
HOGENOMHOG000177963.
KOK00668.
OMAKLQHVGM.
OrthoDBEOG76QFRJ.
PhylomeDBQ9UUG0.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.40.366.10. 5 hits.
InterProIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013785. Aldolase_TIM.
IPR013565. DUF1729.
IPR003965. Fatty_acid_synthase.
IPR016452. Fatty_acid_Synthase_bsu_fun.
IPR002539. MaoC_dom.
[Graphical view]
PfamPF00698. Acyl_transf_1. 1 hit.
PF08354. DUF1729. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PIRSFPIRSF005562. FAS_yeast_beta. 1 hit.
PRINTSPR01483. FASYNTHASE.
SUPFAMSSF52151. SSF52151. 5 hits.
ProtoNetSearch...

Other

NextBio20804508.

Entry information

Entry nameFAS1_SCHPO
AccessionPrimary (citable) accession number: Q9UUG0
Secondary accession number(s): P78799
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names