Q10289 (FAS2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fatty acid synthase subunit alpha
EC=2.3.1.86

Alternative name(s):
p190/210

Including the following 3 domains:

1. Acyl carrier
2. 3-oxoacyl-[acyl-carrier-protein] reductase
   EC=1.1.1.100
   Alternative name(s):
   Beta-ketoacyl reductase
3. 3-oxoacyl-[acyl-carrier-protein] synthase
   EC=2.3.1.41
   Alternative name(s):
   Beta-ketoacyl synthase

Gene names

Name:	fas2
Synonyms:	lsd1
ORF Names:	SPAC4A8.11c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	1842 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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.
Catalytic activity	Acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NAD+ + 2n NADP+. Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
Subunit structure	[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).
Sequence similarities	Belongs to the fungal fatty acid synthetase subunit alpha family. Contains 1 acyl carrier domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Ligand	Magnesium Metal-binding NAD NADP Phosphopantetheine
Molecular function	Oxidoreductase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	macromolecule biosynthetic process Inferred from electronic annotation. Source: InterPro palmitic acid biosynthetic process Inferred from mutant phenotype Ref.2. Source: PomBase regulation of mitosis Inferred from mutant phenotype Ref.1. Source: PomBase
Cellular_component	fatty acid synthase complex Inferred from direct assay PubMed 9693066. Source: PomBase
Molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Inferred from sequence orthology. Source: PomBase 3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from sequence orthology. Source: PomBase fatty-acyl-CoA synthase activity Inferred from electronic annotation. Source: EC holo-[acyl-carrier-protein] synthase activity Inferred from sequence orthology. Source: PomBase magnesium ion binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1842	1842	Fatty acid synthase subunit alpha		PRO_0000180286
Regions
	Domain	134 – 295	162	Acyl carrier
	Region	1728 – 1730	3	Acetyl-CoA binding By similarity
	Region	1773 – 1789	17	Acetyl-CoA binding By similarity
	Region	1797 – 1800	4	Acetyl-CoA binding By similarity
	Region	1827 – 1829	3	Acetyl-CoA binding By similarity
	Region	? – 1842		Beta-ketoacyl synthase
Sites
	Active site	1262	1	For beta-ketoacyl synthase activity By similarity
	Metal binding	1728	1	Magnesium By similarity
	Metal binding	1729	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	1730	1	Magnesium By similarity
	Metal binding	1828	1	Magnesium By similarity
	Metal binding	1829	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	1754	1	Acetyl-CoA By similarity
	Binding site	1764	1	Acetyl-CoA By similarity
Amino acid modifications
	Modified residue	180	1	O-(pantetheine 4'-phosphoryl)serine By similarity
	Modified residue	604	1	Phosphoserine Ref.8
	Modified residue	1412	1	Phosphoserine Ref.8
Natural variations
	Natural variant	4	1	E → V in strain: H265.
	Natural variant	600	1	I → N in strain: H518.
	Natural variant	1276	1	I → T in strain: H201.
Experimental info
	Sequence conflict	107	1	S → A in AAB39943. Ref.4
	Sequence conflict	422	1	K → R in BAA11913. Ref.1
	Sequence conflict	1586	1	P → S in BAA13877. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q10289 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: E4019F2D133EE571	FASTA	1,842	202,169
	10 20 30 40 50 60 MRPEVEQELA HTLLLELLAY QFASPVRWIE TQDVILSPPV SAERIVEIGP SPTLAGMAKR 70 80 90 100 110 120 TLKLKYENMD AALSINREVL CYSKDAREIY YNFEDEVADE PAEAPASTSS TPKVETAAAA 130 140 150 160 170 180 APAATPAPAP AQTSAPAAAL PDEPPKALEV LHTLVAQKLK KSIEEVSPQK SIKDLVGGKS 190 200 210 220 230 240 TLQNEILGDL QKEFGATPEK PEEVPLDELG AIMQSSFNGS LGKQSSSLIS RMISSKMPGG 250 260 270 280 290 300 FNNSAVRGYL GNRYGLGPGR LESVLLLALT MEPASRLGSE ADAKAWLDSV AQKYAARNGV 310 320 330 340 350 360 TLSSPTAEGG SSSGSAAVID EETFKKLTKN NTMLVTQQLE LFARYLNKDL RAGQKAQVAE 370 380 390 400 410 420 KVISDTLRAQ LDLWNEEHGE FYASGIAPIF SPLKARVYDS DWNWARQDAL KMFFDIIFGR 430 440 450 460 470 480 LKHVDTEIVA RCISVMNRSN PTLLEFMQYH IDHCPAEKGE TYQLAKTLGQ QLIDNCKSVI 490 500 510 520 530 540 DAPPVFKNVN HPTAPSTTID ERGNLNYEEI PRPGVRKLTH YVTEMAKGGK LPTESKNKAK 550 560 570 580 590 600 VQNDLARIYR IIKSQNKMSR SSKLQIKQLY GQVLHALSLP LPSSNDEQTP VKETIPFLHI 610 620 630 640 650 660 RKKSVDGNWE FNKSLTGTYL DVLESGAKNG ITYQDKYALV TGAGAGSIGA QIVEGLLAGG 670 680 690 700 710 720 AKVVVTTSRF SRKVTEFYQS LYTRHGSRGS CLIVVPFNQG SKTDVEALID YIYDEKKGLG 730 740 750 760 770 780 WNLDYIVPFA AIPENGREID GIDSRSEFAH RIMLTNILRL LGAVKSQKAS RGMDTRPAQV 790 800 810 820 830 840 ILPLSPNHGT FGNDGLYSES KLGLETLFNR WYSESWANYL TICGAVIGWT RGTGLMAPNN 850 860 870 880 890 900 IVSQGIEKYG VRTFSQSEMA FNILGLMSQK VVDLCQSEPI YANLNGGLEL LPDLKDLSTR 910 920 930 940 950 960 LRTELLETAE IRRAVAAETA FDHSITNGPD SEAVFQKTAI QPRANLKFNF PKLKPYEALS 970 980 990 1000 1010 1020 HLSDLRGMVD LEKVPVVTGF SEVGPWGNSR TRWDMECYGE FSLEGCVEIA WIMGLIKNFN 1030 1040 1050 1060 1070 1080 GKGKDGKPYS GWVDTKTGEP VDDKDVKAKY EKYILEHCGI RIIEAELFHG YNPEKKELLQ 1090 1100 1110 1120 1130 1140 EVVIDHDLEP FEASKEAAHE FKLRHGDQVE IFEIPDSTEW SVRFKRGTSM LIPKALRFDR 1150 1160 1170 1180 1190 1200 FVAGQIPLGW DPKRYGIPDD IISQVDPTTL YVLVSTVEAL VASGITDPYE CYKYIHVSEL 1210 1220 1230 1240 1250 1260 GNTVGSGIGG MSALRGMYKD RWTDKPVQKD ILQESFINTA NAWINMLLLS ASGPIKTPVG 1270 1280 1290 1300 1310 1320 ACATAVESVD AAVDLITSGK ARICISGGYD DFSEEGSYEF ANMGATSNAA KETERGRTPQ 1330 1340 1350 1360 1370 1380 EMSRPATSTR DGFMESQGAG VQIIMQAKLA IEMGVPIHGI VGYVSTAMDK QGRSVPAPGQ 1390 1400 1410 1420 1430 1440 GILTGAREIA TKTPLPIVDL KFRSRQLQRR RSQIGEWAER EYLYLEEELD AMKVQNPDLD 1450 1460 1470 1480 1490 1500 LEAYRIERIN VIKEEVVRQE KEALNTFGNE FWKRDPTIAP IRGALAVWGL TIDDLGVASF 1510 1520 1530 1540 1550 1560 HGTSTKANEK NECDVIDSQL THLGRSKGNA VYGVFQKYLT GHSKGGAGAW MLNGALQILR 1570 1580 1590 1600 1610 1620 SGFVPGNRNA DNIDEYLARF DRVMFPSEGI QTDGIKAASV TAFGFGQVGG QVIVIHPDYI 1630 1640 1650 1660 1670 1680 YGVIDEATYN AYKAKTAARY KASYRYTHDA LVYNNLVRAK DSPPYTKEQE KAVYLNPLAR 1690 1700 1710 1720 1730 1740 ASKSKAGTWT FPATLPAESD ISKTNETTRT LQSLTTSLTN SNENVGVDVE LVSAISIDNE 1750 1760 1770 1780 1790 1800 TFIERNFTDT ERKYCFAAPN PQASFAGRWS AKEAVFKSLG ISGKGAAAPL KDIEIISSES 1810 1820 1830 1840 GAPEVVLHGE AAKAATTAGV KSVSVSISHD DNQSVSVALA HK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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-604 AND SER-1412, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	A54083. T38781. T43037. T43409.
RefSeq	NP_593823.1. NM_001019252.2.
3D structure databases
ProteinModelPortal	Q10289.
SMR	Q10289. Positions 1-94.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q10289. 1 interaction.
STRING	4896.SPAC4A8.11c-1.
Proteomic databases
PRIDE	Q10289.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC4A8.11c.1; SPAC4A8.11c.1:pep; SPAC4A8.11c.
GeneID	2543618.
KEGG	spo:SPAC4A8.11c.
Organism-specific databases
PomBase	SPAC4A8.11c.
Phylogenomic databases
HOGENOM	HOG000177974.
KO	K00667.
OMA	FINTMSA.
OrthoDB	EOG4VHPFG.
Family and domain databases
Gene3D	3.40.366.10. 1 hit. 3.40.47.10. 3 hits. 3.40.50.720. 1 hit. 3.90.470.20. 1 hit.
InterPro	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]
Pfam	PF01648. ACPS. 1 hit. PF00109. ketoacyl-synt. 1 hit. PF02801. Ketoacyl-synt_C. 1 hit. [Graphical view]
PIRSF	PIRSF000454. FAS_yeast_alpha. 1 hit.
ProDom	PD004282. PPantethiene-prot_Trfase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF56214. 4-PPT_transf. 1 hit. SSF52151. Acyl_Trfase/lysoPlipase. 1 hit. SSF53901. Thiolase-like. 2 hits.
TIGRFAMs	TIGR00556. pantethn_trn. 1 hit.
PROSITE	PS50075. ACP_DOMAIN. False negative. PS00606. B_KETOACYL_SYNTHASE. 1 hit. PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20804624.

Entry information

Entry name

FAS2_SCHPO

Accession

Primary (citable) accession number: Q10289
Secondary accession number(s): O14163 , P78866, P78973, Q96WT6, Q96WT7, Q96WT8, Q9URI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	August 14, 2001
Last modified:	May 1, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program