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Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)]

 FAS2_CANPC              Reviewed;        1884 AA.
G8BAW7;
03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
25-JAN-2012, sequence version 1.
25-OCT-2017, entry version 34.
RecName: Full=Fatty acid synthase subunit alpha;
EC=2.3.1.86;
Includes:
RecName: Full=Acyl carrier;
Includes:
RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
EC=1.1.1.100;
AltName: Full=Beta-ketoacyl reductase;
Includes:
RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
EC=2.3.1.41;
AltName: Full=Beta-ketoacyl synthase;
Name=FAS2; OrderedLocusNames=CPAR2_807400;
Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
parapsilosis).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=578454;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CDC 317 / ATCC MYA-4646;
PubMed=19465905; DOI=10.1038/nature08064;
Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L.,
Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S.,
Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D.,
Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E.,
Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J.,
Santos M.C., Schmitzberger F.F., Sherlock G., Shah P.,
Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I.,
Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W.,
Kellis M., Cuomo C.A.;
"Evolution of pathogenicity and sexual reproduction in eight Candida
genomes.";
Nature 459:657-662(2009).
[2]
GENOME REANNOTATION.
STRAIN=CDC 317 / ATCC MYA-4646;
PubMed=22192698; DOI=10.1186/1471-2164-12-628;
Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G.,
Corton N.J., Berriman M., Butler G.;
"Using RNA-seq to determine the transcriptional landscape and the
hypoxic response of the pathogenic yeast Candida parapsilosis.";
BMC Genomics 12:628-628(2011).
[3]
INDUCTION BY HYPOXIA AND BIOFILM FORMATION.
PubMed=19151323; DOI=10.1128/EC.00350-08;
Rossignol T., Ding C., Guida A., d'Enfert C., Higgins D.G., Butler G.;
"Correlation between biofilm formation and the hypoxic response in
Candida parapsilosis.";
Eukaryot. Cell 8:550-559(2009).
[4]
FUNCTION, INDUCTION BY CARBON SOURCES, AND DISRUPTION PHENOTYPE.
PubMed=20027295; DOI=10.1371/journal.pone.0008421;
Nguyen L.N., Trofa D., Nosanchuk J.D.;
"Fatty acid synthase impacts the pathobiology of Candida parapsilosis
in vitro and during mammalian infection.";
PLoS ONE 4:E8421-E8421(2009).
-!- 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. {ECO:0000269|PubMed:20027295}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-
chain-acyl-CoA + n CoA + n CO(2) + 2n NADP(+).
-!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl-
carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) +
[acyl-carrier-protein].
-!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] +
NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
-!- SUBUNIT: Fatty acid synthase is composed of alpha and beta
subunits. {ECO:0000250}.
-!- INDUCTION: Expression significantly elevated by the presence of
glucose. Down-regulated by unsaturated fatty acids oleic acid and
Tween 80. Up-regulated during in vitro biofilm formation and
hypoxic conditions. {ECO:0000269|PubMed:19151323,
ECO:0000269|PubMed:20027295}.
-!- DISRUPTION PHENOTYPE: Essential for growth in fatty acid-free
medium, but dispensable in medium with fatty acids. The growth in
the presence of fatty acid depends on the type. Able to grow in a
concentration-dependent manner in the presence of myristic acid,
palmitic acid, or Tween 80 as the fatty acid sources, but unable
to grow in the presence of unsaturated fatty like acids stearic
acid or oleic acid. Intracellular survival in the murine
macrophage line J774.16 is significantly reduced compared to wild
type or heterozygous fungal cells. Required for systemic infection
in mice. Impaired in its capacity to form biofilms on polysterene
and silicone surfaces. {ECO:0000269|PubMed:20027295}.
-!- MISCELLANEOUS: It can potentially be a fungicidal target.
Inhibition of FAS2 by cerulenin impeds the growth of wild-type and
heterozygous strains (PubMed:20027295).
{ECO:0000305|PubMed:20027295}.
-!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit
alpha family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; HE605205; CCE42191.1; -; Genomic_DNA.
SMR; G8BAW7; -.
EnsemblFungi; CCE42191; CCE42191; CPAR2_807400.
CGD; CAL0000152877; FAS2.
OrthoDB; EOG092C010Q; -.
Proteomes; UP000005221; Chromosome 8.
GO; GO:0005835; C:fatty acid synthase complex; IEA:EnsemblFungi.
GO; GO:0102131; F:3-oxo-glutaryl-[acp] methyl ester reductase activity; IEA:UniProtKB-EC.
GO; GO:0102132; F:3-oxo-pimeloyl-[acp] methyl ester reductase activity; IEA:UniProtKB-EC.
GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0006633; P:fatty acid biosynthetic process; IMP:CGD.
GO; GO:1900535; P:palmitic acid biosynthetic process; IEA:EnsemblFungi.
GO; GO:0009405; P:pathogenesis; IMP:CGD.
GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
Gene3D; 3.40.47.10; -; 2.
Gene3D; 3.90.470.20; -; 1.
HAMAP; MF_00101; AcpS; 1.
InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
InterPro; IPR002582; ACPS.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR026025; FAS_alpha_yeast.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
InterPro; IPR002347; SDR_fam.
InterPro; IPR016039; Thiolase-like.
Pfam; PF01648; ACPS; 1.
Pfam; PF00106; adh_short; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
ProDom; PD004282; PPantethiene-prot_Trfase; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52151; SSF52151; 1.
SUPFAM; SSF53901; SSF53901; 4.
SUPFAM; SSF56214; SSF56214; 1.
TIGRFAMs; TIGR00556; pantethn_trn; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
2: Evidence at transcript level;
Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism;
Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphopantetheine;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 1884 Fatty acid synthase subunit alpha.
/FTId=PRO_0000419251.
DOMAIN 147 222 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
REGION 677 873 Beta-ketoacyl reductase. {ECO:0000250}.
REGION 1147 1361 Beta-ketoacyl synthase. {ECO:0000250}.
REGION 1770 1772 Acetyl-CoA binding. {ECO:0000250}.
REGION 1815 1831 Acetyl-CoA binding. {ECO:0000250}.
REGION 1839 1842 Acetyl-CoA binding. {ECO:0000250}.
REGION 1869 1871 Acetyl-CoA binding. {ECO:0000250}.
ACT_SITE 1303 1303 For beta-ketoacyl synthase activity.
{ECO:0000250}.
METAL 1770 1770 Magnesium. {ECO:0000250}.
METAL 1771 1771 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1772 1772 Magnesium. {ECO:0000250}.
METAL 1870 1870 Magnesium. {ECO:0000250}.
METAL 1871 1871 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
BINDING 1796 1796 Acetyl-CoA. {ECO:0000250}.
BINDING 1806 1806 Acetyl-CoA. {ECO:0000250}.
MOD_RES 182 182 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
SEQUENCE 1884 AA; 206941 MW; 33DCED9F65C58282 CRC64;
MKPEIEQELS HTLLTELLAY QFASPVRWIE TQDVFLKQHN TERVIEIGPS PTLAGMASRT
IKAKYQSYDA ALSLQRQVLC YSKDAKEIYY TPDPAEPPAA EEPKAETGKE SAPAASAAAA
AATQPAAAVA PPPQSAGPVE SIPDEPVKAS LLIHVLVAQK LKKPLDAVPM SKAIKDLVNG
KSTVQNEILG DLGKEFGSTP EKPEETPLEE LAEQFQDTFS GSLGKTSTSL IGRLMSSKMP
GGFSITNARK YLESRFGLGP GRQDSVLLTA LCNEPASRLG SEGDAKSFLD TMAQKYASHA
GISLSSPSAG GASSGAGAAV VDSAALDALI AENKKLARQQ LETLARYLQV DLTKGEKAFI
KEKEATTVLQ QELDLWEAEH GEFYAKGIKP VFSPLKSRTY DSYWNWARQD LLSMWFDILF
GKLTSVDRET INQCIQIMNR ANPTLIKFMQ YHVELCPTYR GETYKLGKRL GEQLIENCKQ
ILGQSPVYKD VSRITGPKTT VSAKGDIVYE EANKESVRKF EQYVFEMAQG GSMTKMKQSS
IQEDLARVYK AISKQASRDS KLELQKVYDQ LLKVVEGSTE IETEQTTQDA LAIPTGSNTP
TEEDELSTAS DDDEIASLPD KTSIAQPVSS TIPNKTIPFL HIQSKSESGN WEYDRKLSSI
YLDGLESAAI NGLTFKDKYV LVTGAGAGSI GAEILQGLIS GGAKVIVTTS RYSKKVTEYY
QNMYARYGAA GSTLIVVPFN QGSKQDVDAL VEYIYNDQKK GGLGWDLDVI IPFAAIPENG
NGIDNIDSKS EFAHRIMLTN LLRLLGAVKA RKTTDTRPAQ CILPLSPNHG TFGFDGLYSE
SKISLETLFN RWYSEDWGTK LTICGAIIGW TRGTGLMSAN NIIAEGIEKL GVRTFSQKEM
AFNILGLLTP EIVNLCQEEP VMADLNGGLQ FIDNLKEFTS KLRNDLTETA DIRRAVSIES
AIEQKVVNGD NVDSNYNKVT VRPRANMKFD FPTLKSYDEI KQIAPDLEGM LDLENVVVVT
GFAEVGPWGN ARTRWEMESK GEFSLEGAIE MAWIMGMIKY HNGNLKGKPY SGWIDAKTQT
PVDDKDIKAK YEEEILEHSG IRLIEPELFN GYDPKKKQMI QEVVIQHDLE PFECSKETAE
QYKHEHGDKC EISEIEESGE YSVRILKGAT LFIPKALRFD RLVAGQIPTG WDARTYGIPE
DTINQVDPIT LYVLVATVEA LLSAGITDPY EFYKYVHVSE VGNCSGSGMG GVSALRGMFK
DRYADKPVQN DILQESFINT MSAWVNMLLL SASGPIKTPV GACATAVESV DIGIETILSG
KAKVVMVGGY DDFQEEGSYE FANMNATSSA IDEFKHGRTP KEMSRPTTTT RNGFMEAQGS
GIQVIMSADL ALKMGVPIHA VLAMSATATD KIGRSVPAPG KGILTTAREH HGNLKYPSPL
LNVKYRKRQL SKRLDQIKSW ESSELNYLQE EAHLAKEEFG EEFSEAEFLR ERTEEIYRES
KRQVADAKKQ WGNAFYKSDP RIAPLRGALA TFNLTIDDIG VASFHGTSTV ANDKNESATI
DSMMKHLGRS EGNPVFGVFQ KYLTGHPKGA AGAWMLNGAI QILESGIVPG NRNADNVDKV
LEQYEYVLYP SRSIQTDGIK AVSVTSFGFG QKGAQAVVVH PDYLYAVLDR STYEDYAKRV
TARNKKTYRY MHNAITRNTM FVAKDKAPYS DELTMDVYLD PLARVSKTKN EFVFTKKSVQ
SDKSYVSNIA NSTAKALSSL NKSSKGVGVD VELLSELNID NETFLERNFT PEEIKYCQNS
ANPQASFTGT WSAKEATFKA LGVSSQGGGA SLKEIEIVRD GNGAPQVVLN DNAKAAAKAA
GVKNVNVSIS HDDFQATAVA LSEF


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