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Q10289

- FAS2_SCHPO

UniProt

Q10289 - FAS2_SCHPO

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Protein

Fatty acid synthase subunit alpha

Gene
fas2, lsd1, SPAC4A8.11c
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.UniRule annotation

Catalytic activityi

Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+.UniRule annotation
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].UniRule annotation
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1262 – 12621For beta-ketoacyl synthase activity By similarity
Metal bindingi1728 – 17281Magnesium By similarity
Metal bindingi1729 – 17291Magnesium; via carbonyl oxygen By similarity
Metal bindingi1730 – 17301Magnesium By similarity
Binding sitei1754 – 17541Acetyl-CoA By similarity
Binding sitei1764 – 17641Acetyl-CoA By similarity
Metal bindingi1828 – 18281Magnesium By similarity
Metal bindingi1829 – 18291Magnesium; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: PomBase
  2. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: PomBase
  3. fatty acid synthase activity Source: PomBase
  4. fatty-acyl-CoA synthase activity Source: UniProtKB-EC
  5. holo-[acyl-carrier-protein] synthase activity Source: PomBase
  6. magnesium ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: PomBase
  2. long-chain fatty acid biosynthetic process Source: PomBase
  3. macromolecule biosynthetic process Source: InterPro
  4. palmitic acid biosynthetic process Source: PomBase
  5. regulation of mitosis Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Magnesium, Metal-binding, NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid synthase subunit alpha (EC:2.3.1.86)
Alternative name(s):
p190/210
Including the following 3 domains:
Acyl carrier
3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.100)
Alternative name(s):
Beta-ketoacyl reductase
3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.41)
Alternative name(s):
Beta-ketoacyl synthase
Gene namesi
Name:fas2
Synonyms:lsd1
ORF Names:SPAC4A8.11c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC4A8.11c.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. fatty acid synthase complex Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18421842Fatty acid synthase subunit alphaUniRule annotationPRO_0000180286Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residuei604 – 6041Phosphoserine1 Publication
Modified residuei1412 – 14121Phosphoserine1 Publication

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

MaxQBiQ10289.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi280032. 6 interactions.
IntActiQ10289. 1 interaction.
MINTiMINT-4698444.
STRINGi4896.SPAC4A8.11c-1.

Structurei

3D structure databases

ProteinModelPortaliQ10289.
SMRiQ10289. Positions 1-94.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini134 – 295162Acyl carrierAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni? – 1842Beta-ketoacyl synthaseUniRule annotation
Regioni1728 – 17303Acetyl-CoA binding By similarity
Regioni1773 – 178917Acetyl-CoA binding By similarityAdd
BLAST
Regioni1797 – 18004Acetyl-CoA binding By similarity
Regioni1827 – 18293Acetyl-CoA binding By similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000177974.
KOiK00667.
OMAiQVIMNAD.
OrthoDBiEOG76QFRJ.
PhylomeDBiQ10289.

Family and domain databases

Gene3Di3.40.366.10. 1 hit.
3.40.47.10. 3 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
HAMAPiMF_00101. AcpS.
InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
IPR001227. Ac_transferase_dom.
IPR002582. ACPS.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR026025. FAS_alpha_yeast.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016040. NAD(P)-bd_dom.
IPR004568. PPantethiene-prot_Trfase_dom.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000454. FAS_yeast_alpha. 1 hit.
ProDomiPD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF52151. SSF52151. 1 hit.
SSF53901. SSF53901. 3 hits.
SSF56214. SSF56214. 1 hit.
TIGRFAMsiTIGR00556. pantethn_trn. 1 hit.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10289-1 [UniParc]FASTAAdd to Basket

« Hide

MRPEVEQELA HTLLLELLAY QFASPVRWIE TQDVILSPPV SAERIVEIGP     50
SPTLAGMAKR TLKLKYENMD AALSINREVL CYSKDAREIY YNFEDEVADE 100
PAEAPASTSS TPKVETAAAA APAATPAPAP AQTSAPAAAL PDEPPKALEV 150
LHTLVAQKLK KSIEEVSPQK SIKDLVGGKS TLQNEILGDL QKEFGATPEK 200
PEEVPLDELG AIMQSSFNGS LGKQSSSLIS RMISSKMPGG FNNSAVRGYL 250
GNRYGLGPGR LESVLLLALT MEPASRLGSE ADAKAWLDSV AQKYAARNGV 300
TLSSPTAEGG SSSGSAAVID EETFKKLTKN NTMLVTQQLE LFARYLNKDL 350
RAGQKAQVAE KVISDTLRAQ LDLWNEEHGE FYASGIAPIF SPLKARVYDS 400
DWNWARQDAL KMFFDIIFGR LKHVDTEIVA RCISVMNRSN PTLLEFMQYH 450
IDHCPAEKGE TYQLAKTLGQ QLIDNCKSVI DAPPVFKNVN HPTAPSTTID 500
ERGNLNYEEI PRPGVRKLTH YVTEMAKGGK LPTESKNKAK VQNDLARIYR 550
IIKSQNKMSR SSKLQIKQLY GQVLHALSLP LPSSNDEQTP VKETIPFLHI 600
RKKSVDGNWE FNKSLTGTYL DVLESGAKNG ITYQDKYALV TGAGAGSIGA 650
QIVEGLLAGG AKVVVTTSRF SRKVTEFYQS LYTRHGSRGS CLIVVPFNQG 700
SKTDVEALID YIYDEKKGLG WNLDYIVPFA AIPENGREID GIDSRSEFAH 750
RIMLTNILRL LGAVKSQKAS RGMDTRPAQV ILPLSPNHGT FGNDGLYSES 800
KLGLETLFNR WYSESWANYL TICGAVIGWT RGTGLMAPNN IVSQGIEKYG 850
VRTFSQSEMA FNILGLMSQK VVDLCQSEPI YANLNGGLEL LPDLKDLSTR 900
LRTELLETAE IRRAVAAETA FDHSITNGPD SEAVFQKTAI QPRANLKFNF 950
PKLKPYEALS HLSDLRGMVD LEKVPVVTGF SEVGPWGNSR TRWDMECYGE 1000
FSLEGCVEIA WIMGLIKNFN GKGKDGKPYS GWVDTKTGEP VDDKDVKAKY 1050
EKYILEHCGI RIIEAELFHG YNPEKKELLQ EVVIDHDLEP FEASKEAAHE 1100
FKLRHGDQVE IFEIPDSTEW SVRFKRGTSM LIPKALRFDR FVAGQIPLGW 1150
DPKRYGIPDD IISQVDPTTL YVLVSTVEAL VASGITDPYE CYKYIHVSEL 1200
GNTVGSGIGG MSALRGMYKD RWTDKPVQKD ILQESFINTA NAWINMLLLS 1250
ASGPIKTPVG ACATAVESVD AAVDLITSGK ARICISGGYD DFSEEGSYEF 1300
ANMGATSNAA KETERGRTPQ EMSRPATSTR DGFMESQGAG VQIIMQAKLA 1350
IEMGVPIHGI VGYVSTAMDK QGRSVPAPGQ GILTGAREIA TKTPLPIVDL 1400
KFRSRQLQRR RSQIGEWAER EYLYLEEELD AMKVQNPDLD LEAYRIERIN 1450
VIKEEVVRQE KEALNTFGNE FWKRDPTIAP IRGALAVWGL TIDDLGVASF 1500
HGTSTKANEK NECDVIDSQL THLGRSKGNA VYGVFQKYLT GHSKGGAGAW 1550
MLNGALQILR SGFVPGNRNA DNIDEYLARF DRVMFPSEGI QTDGIKAASV 1600
TAFGFGQVGG QVIVIHPDYI YGVIDEATYN AYKAKTAARY KASYRYTHDA 1650
LVYNNLVRAK DSPPYTKEQE KAVYLNPLAR ASKSKAGTWT FPATLPAESD 1700
ISKTNETTRT LQSLTTSLTN SNENVGVDVE LVSAISIDNE TFIERNFTDT 1750
ERKYCFAAPN PQASFAGRWS AKEAVFKSLG ISGKGAAAPL KDIEIISSES 1800
GAPEVVLHGE AAKAATTAGV KSVSVSISHD DNQSVSVALA HK 1842
Length:1,842
Mass (Da):202,169
Last modified:August 14, 2001 - v2
Checksum:iE4019F2D133EE571
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41E → V in strain: H265.
Natural varianti600 – 6001I → N in strain: H518.
Natural varianti1276 – 12761I → T in strain: H201.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071S → A in AAB39943. 1 Publication
Sequence conflicti422 – 4221K → R in BAA11913. 1 Publication
Sequence conflicti1586 – 15861P → S in BAA13877. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D83412 Genomic DNA. Translation: BAA11913.1.
AB013747 Genomic DNA. Translation: BAB62029.1.
AB013748 Genomic DNA. Translation: BAB62030.1.
AB013749 Genomic DNA. Translation: BAB62031.1.
AB013750 Genomic DNA. Translation: BAB62032.1.
CU329670 Genomic DNA. Translation: CAB11481.1.
U82216 Genomic DNA. Translation: AAB39943.1.
D89216 mRNA. Translation: BAA13877.1.
U97396 mRNA. Translation: AAB63888.1.
PIRiA54083.
T38781.
T43037.
T43409.
RefSeqiNP_593823.1. NM_001019252.2.

Genome annotation databases

EnsemblFungiiSPAC4A8.11c.1; SPAC4A8.11c.1:pep; SPAC4A8.11c.
GeneIDi2543618.
KEGGispo:SPAC4A8.11c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D83412 Genomic DNA. Translation: BAA11913.1 .
AB013747 Genomic DNA. Translation: BAB62029.1 .
AB013748 Genomic DNA. Translation: BAB62030.1 .
AB013749 Genomic DNA. Translation: BAB62031.1 .
AB013750 Genomic DNA. Translation: BAB62032.1 .
CU329670 Genomic DNA. Translation: CAB11481.1 .
U82216 Genomic DNA. Translation: AAB39943.1 .
D89216 mRNA. Translation: BAA13877.1 .
U97396 mRNA. Translation: AAB63888.1 .
PIRi A54083.
T38781.
T43037.
T43409.
RefSeqi NP_593823.1. NM_001019252.2.

3D structure databases

ProteinModelPortali Q10289.
SMRi Q10289. Positions 1-94.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 280032. 6 interactions.
IntActi Q10289. 1 interaction.
MINTi MINT-4698444.
STRINGi 4896.SPAC4A8.11c-1.

Proteomic databases

MaxQBi Q10289.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC4A8.11c.1 ; SPAC4A8.11c.1:pep ; SPAC4A8.11c .
GeneIDi 2543618.
KEGGi spo:SPAC4A8.11c.

Organism-specific databases

PomBasei SPAC4A8.11c.

Phylogenomic databases

HOGENOMi HOG000177974.
KOi K00667.
OMAi QVIMNAD.
OrthoDBi EOG76QFRJ.
PhylomeDBi Q10289.

Miscellaneous databases

NextBioi 20804624.

Family and domain databases

Gene3Di 3.40.366.10. 1 hit.
3.40.47.10. 3 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
HAMAPi MF_00101. AcpS.
InterProi IPR008278. 4-PPantetheinyl_Trfase_SF.
IPR001227. Ac_transferase_dom.
IPR002582. ACPS.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR026025. FAS_alpha_yeast.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016040. NAD(P)-bd_dom.
IPR004568. PPantethiene-prot_Trfase_dom.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000454. FAS_yeast_alpha. 1 hit.
ProDomi PD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF52151. SSF52151. 1 hit.
SSF53901. SSF53901. 3 hits.
SSF56214. SSF56214. 1 hit.
TIGRFAMsi TIGR00556. pantethn_trn. 1 hit.
PROSITEi PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase."
    Saitoh S., Takahashi K., Nabeshima K., Yamashita Y., Nakaseko Y., Hirata A., Yanagida M.
    J. Cell Biol. 134:949-961(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Very long-chain fatty-acid-containing phospholipids accumulate in fatty acid synthase temperature-sensitive mutant strains of the fission yeast Schizosaccharomyces pombe fas2/lsd1."
    Yokoyama K., Saitoh S., Ishida M., Yamakawa Y., Nakamura K., Inoue K., Taguchi R., Tokumura A., Nishijima M., Yanagida M., Setaka M.
    Biochim. Biophys. Acta 1532:223-233(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843, H201, H265 and H518.
  3. "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.
    , 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.
  4. Koken M.H.M., de Rooij J.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-215.
  5. "Schizosaccharomyces pombe fatty acid synthase mediates DNA strand exchange in vitro."
    Kaeslin E., Heyer W.-D.
    J. Biol. Chem. 269:14103-14110(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20.
  6. "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 1466-1842.
    Strain: PR745.
  7. Jang Y.-J., Yoo H.-S.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1505-1564.
    Strain: 972 / ATCC 24843.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604 AND SER-1412, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiFAS2_SCHPO
AccessioniPrimary (citable) accession number: Q10289
Secondary accession number(s): O14163
, P78866, P78973, Q96WT6, Q96WT7, Q96WT8, Q9URI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 14, 2001
Last modified: May 14, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi