3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
     (EC 4.2.1.61)
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)

Gene name

	Name:	fas1
	ORFNames:	SPAC926.09c

From

Schizosaccharomyces pombe (Fission yeast)

[TaxID: 4896]

Taxonomy

Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT. DOI=10.1006/prep.1998.0914; PubMed=9693066 [NCBI, ExPASy, EBI, Israel, Japan] Niwa H., Katayama E., Yanagida M., Morikawa K.; "Cloning of the fatty acid synthetase beta subunit from fission yeast, coexpression with the alpha subunit, and purification of the intact multifunctional enzyme complex."; Protein Expr. Purif. 13:403-413(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 38366 / 972; DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The genome sequence of Schizosaccharomyces pombe."; Nature 415:871-880(2002).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1725-2073. STRAIN=PR745; DOI=10.1093/dnares/4.6.363; PubMed=9501991 [NCBI, ExPASy, EBI, Israel, Japan] Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.; "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."; DNA Res. 4:363-369(1997).
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1122 AND SER-2073, AND MASS SPECTROMETRY. DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan] Wilson-Grady J.T., Villen J., Gygi S.P.; "Phosphoproteome analysis of fission yeast."; J. Proteome Res. 7:1088-1097(2008).

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⁺.
CATALYTIC ACTIVITY: Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].
CATALYTIC ACTIVITY: Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein].
CATALYTIC ACTIVITY: (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] = hexadec-2-enoyl-[acyl-carrier-protein] + H₂O.
CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + NAD⁺ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
CATALYTIC ACTIVITY: Oleoyl-[acyl-carrier-protein] + H₂O = [acyl-carrier-protein] + oleate.
SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits (alpha and beta).
SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB010274; BAA36384.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329670; CAB54157.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D89148; BAA13810.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T39207; T39207.
T42424; T42424.
T43311; T43311.

RefSeq

NP_594370.1; -.

3D structure databases

ModBase

Q9UUG0.

Enzyme and pathway databases

BioCyc

SPOM-XXX-01:SPOM-XXX-01-002475-MON; -.

Organism-specific databases

GeneDB_Spombe

SPAC926.09c; -.

Gene expression databases

ArrayExpress

Q9UUG0; -.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0005835;	Cellular component: fatty acid synthase complex (inferred from electronic annotation from InterPro).
GO:0004317;	Molecular function: 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity (inferred from electronic annotation from EC).
GO:0004313;	Molecular function: [acyl-carrier-protein] S-acetyltransferase activity (inferred from electronic annotation from EC).
GO:0004314;	Molecular function: [acyl-carrier-protein] S-malonyltransferase activity (inferred from electronic annotation from EC).
GO:0004318;	Molecular function: enoyl-[acyl-carrier-protein] reductase (NADH) activity (inferred from electronic annotation from EC).
GO:0004321;	Molecular function: fatty-acyl-CoA synthase activity (inferred from electronic annotation from EC).
GO:0004320;	Molecular function: oleoyl-[acyl-carrier-protein] hydrolase activity (inferred from electronic annotation from EC).
GO:0006633;	Biological process: fatty acid biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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 of domain structure.

Gene3D

G3DSA:3.40.366.10; Ac_transferase_reg; 2.

Pfam

PF00698; Acyl_transf_1; 1.
PF08354; DUF1729; 1.
PF01575; MaoC_dehydratas; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF005562; FAS_yeast_beta; 1.

PR01483; FASYNTHASE.

Genome annotation databases

GeneID

2543497; -.

KEGG

spo:SPAC926.09c; -.

NMPDR

fig|4896.1.peg.4340; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Fatty acid biosynthesis; Hydrolase; Lipid synthesis; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphoprotein; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 2073`	`2073`	`Fatty acid synthase subunit beta.`	`PRO_0000180281`
`REGION`	`1 459`	`459`	`Acetyltransferase.`
`REGION`	`470 858`	`389`	`Enoyl reductase.`
`REGION`	`1155 1644`	`490`	`Dehydratase.`
`REGION`	`1645 2073`	`429`	`Malonyl/palmitoyl transferase.`
`ACT_SITE`	`270 270`		`For acetyltransferase activity (By similarity).`
`ACT_SITE`	`1361 1361`		`For dehydratase activity (Potential).`
`ACT_SITE`	`1828 1828`		`For malonyltransferase activity (By similarity).`
`MOD_RES`	`1122 1122`		`Phosphoserine.`
`MOD_RES`	`2073 2073`		`Phosphoserine.`
`CONFLICT`	`222 222`		`P -> R (in Ref. 1; BAA36384).`

Sequence information

Length: 2073 AA [This is the length of the unprocessed precursor]

Molecular weight: 230561 Da [This is the MW of the unprocessed precursor]

CRC64: D928270838E7C7C4 [This is a checksum on the sequence]

        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

Q9UUG0 in FASTA format

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View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools