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UniProtKB/Swiss-Prot entry P34731

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

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Entry information
Entry name FAS1_CANAL
Primary accession number P34731
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 60)
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
From
Candida albicans (Yeast) [TaxID: 5476] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=4918;
DOI=10.1016/0378-1119(94)90050-7; PubMed=8088535 [NCBI, ExPASy, EBI, Israel, Japan]
Zhao X.-J., Cihlar R.L.;
"Isolation and sequence of the Candida albicans FAS1 gene.";
Gene 147:119-124(1994).
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
X74952; CAA52907.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S37178; S37178.
3D structure databases
ModBase P34731.
Ontologies
GO
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.
PRINTS PR01483; FASYNTHASE.
ProtoNet P34731.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
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   2037  2037     Fatty acid synthase subunit beta. PRO_0000180280
REGION   1    453  453     Acetyltransferase (By similarity). 
REGION   465    798  334     Enoyl reductase (By similarity). 
REGION   1132   1612  481     Dehydratase (By similarity). 
REGION   1613   1833  221     Malonyl/palmitoyl transferase (By similarity). 
ACT_SITE   261    261        For acetyltransferase activity (By similarity). 
ACT_SITE   1796   1796        For malonyltransferase activity (By similarity). 
Sequence information
Length: 2037 AA [This is the length of the unprocessed precursor] Molecular weight: 227919 Da [This is the MW of the unprocessed precursor] CRC64: D37BDD0DB9A8ADDA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSTHRPFQLT HGSIEHTLLV PNDLFFNYSQ LKDEFIKTLP EPTEGFAGDD EPSSPAELYG 

        70         80         90        100        110        120 
KFIGFISNAQ FPQIVELSLK DFESRFLDNN NDNIHSFAVK LLDDETYPTT IAKVKENIVK 

       130        140        150        160        170        180 
NYYKAVKSIN KVESNLLYHC KHDAKLVAIF GGQGNTDDYF EELRELYTLY QGLIEDLLVS 

       190        200        210        220        230        240 
IAEKLNQLHP SFDKIYTQGL NILSWLKHPE TTPDQDYLLS VPVSCPVICV IQLCHYTITC 

       250        260        270        280        290        300 
KVLGLTPGEF RNSLKWSTGH SQGLVTAVTI AASDSWDSFL KNSLTAVSLL LFIGSRCLST 

       310        320        330        340        350        360 
YPRTSLPPTM LQDSLDNGEG RPSPMLSVRD LSIKQVEKFI EQTNSHLPRE KHIAISLING 

       370        380        390        400        410        420 
ARNLVLSGPP ESLYGFNLNL RNQKAPMGLD QSRVPFSERK LKCSNRFLPI FAPFHSHLLA 

       430        440        450        460        470        480 
DATELILDDV KEHGLSFEGL KIPVYDTFDG SDFQALKEPI IDRVVKLITE LPVHWEEATN 

       490        500        510        520        530        540 
HKATHILDFG PGGVSGLGVL THRNKEGTGA RIILAGTLDS NPIDDEYGFK HEIFQTSADK 

       550        560        570        580        590        600 
AIKWAPDWLK ELRPTLVKNS EGKIYVKTKF SQLLGRAPLM VAGMTPTTVN TDIVSASLNA 

       610        620        630        640        650        660 
GYHIELAGGG YFSPVMMTRA IDDIVSRIKP GYGLGINLIY VNPFMLQWGI PLIKDLREKG 

       670        680        690        700        710        720 
YPIQSLTIGA GVPSIEVATE YIEDLGLTHL GLKPGSVDAI SQVIAIAKAH PTFPIVLQWT 

       730        740        750        760        770        780 
GGRGGGHHSF EDFHQPIIQM YSKIRRCSNI VLVAGSGFGS DEDTYPYLSG YWSEKFNYPP 

       790        800        810        820        830        840 
MPFDGVLFGS RVMTSKESHT SLAAKKLIVE CKGVPDQQWE QTYKKPTGGI ITVRSEMGEP 

       850        860        870        880        890        900 
IHKIATRGVM FWKELDDTIF NLPKNKLLDA LNKKRDHIIK KLNNDFQKPW FGKNANGVCD 

       910        920        930        940        950        960 
LQEMTYKEVA NRLVELMYVK KSHRWIDVSL RNMYGDFLRR VEERFTSSAG TVSLLQNFNQ 

       970        980        990       1000       1010       1020 
LNEPEQFTAD FFEKFPQAGK QLISEEDCDY FLMLAARPGQ KPVPFVPVLD ERFEFFFKKD 

      1030       1040       1050       1060       1070       1080 
SLWQSEDLES VVDEDVQRTC ILHGPVASQY TSKVDEPIGD ILNSIHEGHI ARLIKEEYAG 

      1090       1100       1110       1120       1130       1140 
DESKIPVVEY FGGKKPASVS ATSVNIIDGN QVVYEIDSEL PNKQEWLDLL AGTELNWLQA 

      1150       1160       1170       1180       1190       1200 
FISTDRIVQG SKHVSNPLHD ILTPAKHSKV TIDKKTKKLT AFENIKGDLL PVVEIELVKP 

      1210       1220       1230       1240       1250       1260 
NTIQLSLIEH RTADTNPVAL PFLYKYNPAD GFAPILEIME DRNERIKEFY WKLWFGSSVP 

      1270       1280       1290       1300       1310       1320 
YSNDINVEKA ILGDEITISS QTISEFTHAI GNKCDAFVDR PGKATLAPMD FAIVIGWKAI 

      1330       1340       1350       1360       1370       1380 
IKAIFPKSVD GDLLKLVHLS NGYKMITGAA PLKKGDVVST KAEIKAVLNQ PSGKLVEVVG 

      1390       1400       1410       1420       1430       1440 
TIYREGKPVM EVTSQFLYRG EYNDYCNTFQ KVTETPVQVA FKSAKDLAVL RSKEWFHLEK 

      1450       1460       1470       1480       1490       1500 
DVQFDVLTFR CESTYKFKSA NVYSSIKTTG QVLLELPTKE VIQVGSVDYE AGTSYGNPVT 

      1510       1520       1530       1540       1550       1560 
DYLSRNGKTI EESVIFENAI PLSSGEELTS KAPGTNEPYA IVSGDYNPIH VSRVFAAYAK 

      1570       1580       1590       1600       1610       1620 
LPGTITHGMY SSASIRALVE EWAANNVAAR VRAFKCDFVG MVLPNDTLQT TMEHVGMING 

      1630       1640       1650       1660       1670       1680 
RKIIKVETRN VETELPVLIG EAEIEQPTTT YVFTGQGSQE QGMGMELYNS SEVAREVWDK 

      1690       1700       1710       1720       1730       1740 
ADRHFVNNYG FSILDIVQNN PNELTIHFGG AKGRAIRDNY IGMMFETIGE DGALKSEKIF 

      1750       1760       1770       1780       1790       1800 
KDIDETTTSY TFVSPTGLLS ATQFTQPALT LMEKAAYEDI KSKGLIPSDI MFAGHSLGEY 

      1810       1820       1830       1840       1850       1860 
SALSSLANVM PIESLVDVVF YRGMTMQVAV PRDELGRSNY GMVAVNPSRV SATFDDSALR 

      1870       1880       1890       1900       1910       1920 
FVVDEVANKT KWLLEIVNYN VENQQYVAAG DLRALDTLTN VLNVLKINKI DIVKLQEQMS 

      1930       1940       1950       1960       1970       1980 
IEKVKEHLYE IVDEVAAKSL AKPQPIDLER GFAVIPLKGI SVPFHSSYLM SGVKPFQRFL 

      1990       2000       2010       2020       2030 
CKKIPKSSVK PQDLIGKYIP NLTAKPFELT KEYFQSVYDL TKSEKIKSIL DNWEQYE
P34731 in FASTA format

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