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Reviewed, UniProtKB/Swiss-Prot P34731 (FAS1_CANAL)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length2037 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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).

Sequence similarities

Belongs to the fungal fatty acid synthetase subunit beta family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20372037Fatty acid synthase subunit beta
PRO_0000180280

Regions

Region1 – 453453Acetyltransferase By similarity
Region465 – 798334Enoyl reductase By similarity
Region1132 – 1612481Dehydratase By similarity
Region1613 – 1833221Malonyl/palmitoyl transferase By similarity

Sites

Active site2611For acetyltransferase activity By similarity
Active site17961For malonyltransferase activity By similarity

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Sequences

Sequence LengthMass (Da)Tools
P34731-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: D37BDD0DB9A8ADDA

FASTA2,037227,919
        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

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References

[1]"Isolation and sequence of the Candida albicans FAS1 gene."
Zhao X.-J., Cihlar R.L.
Gene 147:119-124(1994) [PubMed: 8088535] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 4918.

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Cross-references

Sequence databases

X74952 Genomic DNA. Translation: CAA52907.1.
PIRS37178.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.3.1.9. 1124.
2.3.1.38. 1124.
2.3.1.39. 1124.
2.3.1.86. 1124.
3.1.2.14. 1124.
4.2.1.61. 1124.

Family and domain databases

InterProIPR001227. Ac_transferase_reg.
IPR014043. Acyl_transferase.
IPR013565. DUF1729.
IPR003965. Fatty_acid_synthase.
IPR016452. Fatty_acid_Synthase_bsu_fun.
IPR002539. MaoC_deHydtase.
[Graphical view]
Gene3DG3DSA:3.40.366.10. Ac_transferase_reg. 2 hits.
PfamPF00698. Acyl_transf_1. 1 hit.
PF08354. DUF1729. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PIRSFPIRSF005562. FAS_yeast_beta. 1 hit.
PRINTSPR01483. FASYNTHASE.
ProtoNetSearch...

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Entry information

Entry nameFAS1_CANAL
AccessionPrimary (citable) accession number: P34731
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Candida albicans

Candida albicans: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents