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P34229 (FAS1_YARLI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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. 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
    EC=4.2.1.59
  2. Enoyl-[acyl-carrier-protein] reductase [NADH]
    EC=1.3.1.9
  3. [Acyl-carrier-protein] acetyltransferase
    EC=2.3.1.38
  4. [Acyl-carrier-protein] malonyltransferase
    EC=2.3.1.39
  5. S-acyl fatty acid synthase thioesterase
    EC=3.1.2.14
Gene names
Name:FAS1
Ordered Locus Names:YALI0B15059g
OrganismYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome]
Taxonomic identifier284591 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia

Protein attributes

Sequence length2086 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+.

Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].

Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein].

A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.

An acyl-[acyl-carrier protein] + NAD+ = a 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.

Contains 1 MaoC-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20862086Fatty acid synthase subunit beta
PRO_0000180283

Regions

Domain1550 – 1680131MaoC-like
Region1 – 480480Acetyltransferase
Region492 – 879388Enoyl reductase
Region1166 – 1657492Dehydratase
Region1658 – 1879222Malonyl/palmitoyl transferase

Sites

Active site2861For acetyltransferase activity By similarity
Active site18421For malonyltransferase activity By similarity

Experimental info

Sequence conflict1 – 1111MYPTTGVNTPQ → M in CAA42211. Ref.1
Sequence conflict529 – 5302HK → TR in CAA42211. Ref.1
Sequence conflict12401V → G in CAA42211. Ref.1
Sequence conflict16121H → Q in CAA42211. Ref.1
Sequence conflict20771N → D in CAA42211. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P34229 [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: 060F6CEA44F235B2

FASTA2,086231,342
        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 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59690 Genomic DNA. Translation: CAA42211.1.
CR382128 Genomic DNA. Translation: CAG83163.1.
PIRS15999.
RefSeqXP_500912.1. XM_500912.1.

3D structure databases

ProteinModelPortalP34229.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4952.P34229.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCAG83163; CAG83163; YALI0_B15059g.
GeneID2907339.
KEGGyli:YALI0B15059g.

Phylogenomic databases

eggNOGCOG0331.
HOGENOMHOG000177963.
KOK00668.
OMAKLQHVGM.
OrthoDBEOG76QFRJ.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.40.366.10. 5 hits.
InterProIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013785. Aldolase_TIM.
IPR013565. DUF1729.
IPR003965. Fatty_acid_synthase.
IPR016452. Fatty_acid_Synthase_bsu_fun.
IPR002539. MaoC_dom.
[Graphical view]
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.
SUPFAMSSF52151. SSF52151. 5 hits.
ProtoNetSearch...

Entry information

Entry nameFAS1_YARLI
AccessionPrimary (citable) accession number: P34229
Secondary accession number(s): Q6CEK0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 11, 2004
Last modified: March 19, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families