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UniProtKB/Swiss-Prot entry P34229

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FAS1_YARLI
Primary accession number P34229
Secondary accession number Q6CEK0
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on October 11, 2004 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 64)
Name and origin of the protein
Protein name Fatty acid synthase subunit beta
Synonym EC 2.3.1.86
Includes 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
OrderedLocusNames: YALI0B15059g
From
Yarrowia lipolytica (Candida lipolytica) [TaxID: 4952] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 32338 / CX-161-1B;
DOI=10.1007/BF00273618; PubMed=2034224 [NCBI, ExPASy, EBI, Israel, Japan]
Koettig H., Rottner G., Beck K.-F., Schweizer M., Schweizer E.;
"The pentafunctional FAS1 genes of Saccharomyces cerevisiae and Yarrowia lipolytica are co-linear and considerably longer than previously estimated.";
Mol. Gen. Genet. 226:310-314(1991).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CLIB 122 / E 150;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
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
X59690; CAA42211.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382128; CAG83163.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S15999; S15999.
RefSeq XP_500912.1; -.
3D structure databases
ModBase P34229.
Ontologies
GO
GO:0005835; Cellular component: fatty acid synthase complex (non-traceable author statement from UniProtKB).
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 (non-traceable author statement from UniProtKB).
GO:0004320; Molecular function: oleoyl-[acyl-carrier-protein] hydrolase activity (inferred from electronic annotation from EC).
GO:0006633; Biological process: fatty acid biosynthetic process (non-traceable author statement from UniProtKB).
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.
PRINTS PR01483; FASYNTHASE.
ProtoNet P34229.
Genome annotation databases
GeneID 2907339; -.
KEGG yli:YALI0B15059g; -.
Phylogenomic databases
HOGENOM P34229; -.
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; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   2086  2086     Fatty acid synthase subunit beta. PRO_0000180283
REGION   1    480  480     Acetyltransferase. 
REGION   492    879  388     Enoyl reductase. 
REGION   1166   1657  492     Dehydratase. 
REGION   1658   1879  222     Malonyl/palmitoyl transferase. 
ACT_SITE   286    286        For acetyltransferase activity (By similarity). 
ACT_SITE   1842   1842        For malonyltransferase activity (By similarity). 
CONFLICT   1     11        MYPTTGVNTPQ -> M (in Ref. 1). 
CONFLICT   529    530        HK -> TR (in Ref. 1; CAA42211). 
CONFLICT   1240   1240        V -> G (in Ref. 1; CAA42211). 
CONFLICT   1612   1612        H -> Q (in Ref. 1; CAA42211). 
CONFLICT   2077   2077        N -> D (in Ref. 1; CAA42211). 
Sequence information
Length: 2086 AA [This is the length of the unprocessed precursor] Molecular weight: 231342 Da [This is the MW of the unprocessed precursor] CRC64: 060F6CEA44F235B2 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MYPTTGVNTP QSAASLRPLV LSHGQTEHSL LVPTSLYINC TTLRDQFYAS LPPATEDKAD 

        70         80         90        100        110        120 
DDEPSSSTEL LAAFLGFTAK TVEEEPGPYD DVLSLVLNEF ETRYLRGNDI HAVASSLLQD 

       130        140        150        160        170        180 
EDVPTTVGKI KRVIRAYYAA RIACNRPIKA HSSALFRAAS EDSDNVSLYA IFGGQGNTED 

       190        200        210        220        230        240 
YFEELREIYD IYQGLVGDFI RECGAQLLAL SRDHIAAEKI YTKGFDIVKW LEHPETIPDF 

       250        260        270        280        290        300 
EYLISAPISV PIIGVIQLAH YAVTCRVLGL NPGQVRDNLK GATGHSQGLI TAIAISASDS 

       310        320        330        340        350        360 
WDEFYNSASR ILKIFFFIGV RVQQAYPSTF LPPSTLEDSV KQGEGKPTPM LSIRDLSLNQ 

       370        380        390        400        410        420 
VQEFVDATNL HLPEDKQIVV SLINGPRNVV VTGPPQSLYG LCLVLRKQKA ETGLDQSRVP 

       430        440        450        460        470        480 
HSQRKLKFTH RFLPITSPFH SYLLEKSTDL IINDLESSGV EFVSSELKVP VYDTFDGSVL 

       490        500        510        520        530        540 
SQLPKGIVSR LVNLITHLPV KWEKATQFQA SHIVDFGPGG ASGLGLLTHK NKDGTGVRTI 

       550        560        570        580        590        600 
LAGVIDQPLE FGFKQELFDR QESSIVFAQN WAKEFSPKLV KISSTNEVYV DTKFSRLTGR 

       610        620        630        640        650        660 
APIMVAGMTP TTVNPKFVAA TMNSGYHIEL GGGGYFAPGM MTKALEHIEK NTPPGSGITI 

       670        680        690        700        710        720 
NLIYVNPRLI QWGIPLIQEL RQKGFPIEGL TIGAGVPSLE VANEWIQDLG VKHIAFKPGS 

       730        740        750        760        770        780 
IEAISSVIRI AKANPDFPII LQWTGGRGGG HHSFEDFHAP ILQMYSKIRR CSNIVLIAGS 

       790        800        810        820        830        840 
GFGASTDSYP YLTGSWSRDF DYPPMPFDGI LVGSRVMVAK EAFTSLGAKQ LIVDSPGVED 

       850        860        870        880        890        900 
SEWEKTYDKP TGGVITVLSE MGEPIHKLAT RGVLFWHEMD KTVFSLPKKK RLEVLKSKRA 

       910        920        930        940        950        960 
YIIKRLNDDF QKTWFAKNAQ GQVCDLEDLT YAEVIQRLVD LMYVKKESRW IDVTLRNLAG 

       970        980        990       1000       1010       1020 
TFIRRVEERF STETGASSVL QSFSELDSEP EKVVERVFEL FPASTTQIIN AQDKDHFLML 

      1030       1040       1050       1060       1070       1080 
CLNPMQKPVP FIPVLDDNFE FFFKKDSLWQ CEDLAAVVDE DVGRICILQG PVAVKHSKIV 

      1090       1100       1110       1120       1130       1140 
NEPVKEILDS MHEGHIKQLL EDGEYAGNMA NIPQVECFGG KPAQNFGDVA LDSVMVLDDL 

      1150       1160       1170       1180       1190       1200 
NKTVFKIETG TSALPSAADW FSLLAGDKNS WRQVFLSTDT IVQTTKMISN PLHRLLEPIA 

      1210       1220       1230       1240       1250       1260 
GLQVEIEHPD EPENTVISAF EPINGKVTKV LELRKGAGDV ISLQLIEARG VDRVPVALPL 

      1270       1280       1290       1300       1310       1320 
EFKYQPQIGY APIVEVMTDR NTRIKEFYWK LWFGQDSKFE IDTDITEEII GDDVTISGKA 

      1330       1340       1350       1360       1370       1380 
IADFVHAVGN KGEAFVGRST SAGTVFAPMD FAIVLGWKAI IKAIFPRAID ADILRLVHLS 

      1390       1400       1410       1420       1430       1440 
NGFKMMPGAD PLQMGDVVSA TAKIDTVKNS ATGKTVAVRG LLTRDGKPVM EVVSEFFYRG 

      1450       1460       1470       1480       1490       1500 
EFSDFQNTFE RREEVPMQLT LKDAKAVAIL CSKEWFEYNG DDTKDLEGKT IVFRNSSFIK 

      1510       1520       1530       1540       1550       1560 
YKNETVFSSV HTTGKVLMEL PSKEVIEIAT VNYQAGESHG NPVIDYLERN GTTIEQPVEF 

      1570       1580       1590       1600       1610       1620 
EKPIPLSKAD DLLSFKAPSS NEPYAGVSGD YNPIHVSRAF ASYASLPGTI THGMYSSAAV 

      1630       1640       1650       1660       1670       1680 
RSLIEVWAAE NNVSRVRAFS CQFQGMVLPN DEIVTRLEHV GMINGRKIIK VTSTNRETEA 

      1690       1700       1710       1720       1730       1740 
VVLSGEAEVE QPISTFVFTG QGSQEQGMGM DLYASSEVAK KVWDKADEHF LQNYGFSIIK 

      1750       1760       1770       1780       1790       1800 
IVVENPKELD IHFGGPKGKK IRDNYISMMF ETIDEKTGNL ISEKIFKEID ETTDSFTFKS 

      1810       1820       1830       1840       1850       1860 
PTGLLSATQF TQPALTLMEK ASFEDMKAKG LVPVDATFAG HSLGEYSALA SLGDVMPIES 

      1870       1880       1890       1900       1910       1920 
LVDVVFYRGM TMQVAVPRDA QGRSNYGMCA VNPSRISTTF NDAALRFVVD HISEQTKWLL 

      1930       1940       1950       1960       1970       1980 
EIVNYNVENS QYVTAGDLRA LDTLTNVLNV LKLEKINIDK LLESLPLEKV KEHLSEIVTE 

      1990       2000       2010       2020       2030       2040 
VAKKSVAKPQ PIELERGFAV IPLKGISVPF HSSYLRNGVK PFQNFLVKKV PKNAVKPANL 

      2050       2060       2070       2080 
IGKYIPNLTA KPFEITKEYF EEVYKLTGSE KVKSIINNWE SYESKQ
P34229 in FASTA format

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