Reviewed, UniProtKB/Swiss-Prot Q9UUG0 (FAS1_SCHPO)

Names and origin

Protein names

Recommended name:
    Fatty acid synthase subunit beta
    EC=2.3.1.86
Including the following 5 domains:
    1- Recommended name:
            3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
              EC=4.2.1.61
    2- Recommended name:
            Enoyl-[acyl-carrier-protein] reductase [NADH]
              EC=1.3.1.9
    3- Recommended name:
            [Acyl-carrier-protein] acetyltransferase
              EC=2.3.1.38
    4- Recommended name:
            [Acyl-carrier-protein] malonyltransferase
              EC=2.3.1.39
    5- Recommended name:
            S-acyl fatty acid synthase thioesterase
              EC=3.1.2.14

Gene names

Name:	fas1
ORF Names:	SPAC926.09c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	2073 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 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 NADH + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NAD+ + 2n NADP+. Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein]. Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein]. (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] = hexadec-2-enoyl-[acyl-carrier-protein] + H2O. Acyl-[acyl-carrier-protein] + NAD+ = 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.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Ligand	NAD NADP
Molecular function	Hydrolase Lyase Oxidoreductase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe fatty acid synthase complex Ref.1 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Inferred from electronic annotation. Source: EC [acyl-carrier-protein] S-acetyltransferase activity Inferred from electronic annotation. Source: EC [acyl-carrier-protein] S-malonyltransferase activity Inferred from electronic annotation. Source: EC enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from electronic annotation. Source: EC fatty-acyl-CoA synthase activity Inferred from electronic annotation. Source: EC oleoyl-[acyl-carrier-protein] hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2073	2073	Fatty acid synthase subunit beta		PRO_0000180281
Regions
	Region	1 – 459	459	Acetyltransferase
	Region	470 – 858	389	Enoyl reductase
	Region	1155 – 1644	490	Dehydratase
	Region	1645 – 2073	429	Malonyl/palmitoyl transferase
Sites
	Active site	270	1	For acetyltransferase activity By similarity
	Active site	1361	1	For dehydratase activity Potential
	Active site	1828	1	For malonyltransferase activity By similarity
Amino acid modifications
	Modified residue	1122	1	Phosphoserine Ref.4
	Modified residue	2073	1	Phosphoserine Ref.4
Experimental info
	Sequence conflict	222	1	P → R in BAA36384. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UUG0-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: D928270838E7C7C4	FASTA	2,073	230,561
	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

References

	« Hide 'large scale' referencesShow '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: 9693066] [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. , 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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[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: 9501991] [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: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1122 AND SER-2073, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB010274 Genomic DNA. Translation: BAA36384.1. CU329670 Genomic DNA. Translation: CAB54157.1. D89148 mRNA. Translation: BAA13810.1.
PIR	T39207. T42424. T43311.
RefSeq	NP_594370.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2543497.
KEGG	spo:SPAC926.09c.
NMPDR	fig|4896.1.peg.4340.
Organism-specific databases
GeneDB_Spombe	SPAC926.09c.
Phylogenomic databases
OMA	Q9UUG0. SATQFTQ.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002475-MON.
BRENDA	1.3.1.9. 653. 2.3.1.38. 653. 2.3.1.39. 653. 2.3.1.86. 653. 3.1.2.14. 653. 4.2.1.61. 653.
Gene expression databases
ArrayExpress	Q9UUG0.
Family and domain databases
InterPro	IPR001227. Ac_transferase_reg. IPR014043. Acyl_transferase. IPR013565. DUF1729. IPR003965. Fatty_acid_synthase. IPR016452. Fatty_acid_Synthase_bsu_fun. IPR002539. MaoC_deHydtase. [Graphical view]
Gene3D	G3DSA:3.40.366.10. Ac_transferase_reg. 2 hits.
Pfam	PF00698. Acyl_transf_1. 1 hit. PF08354. DUF1729. 1 hit. PF01575. MaoC_dehydratas. 1 hit. [Graphical view]
PIRSF	PIRSF005562. FAS_yeast_beta. 1 hit.
PRINTS	PR01483. FASYNTHASE.
ProtoNet	Search...

Entry information

Entry name

FAS1_SCHPO

Accession

Primary (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:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)