Fatty acid synthase - Bos taurus (Bovine)

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Reviewed, UniProtKB/Swiss-Prot Q71SP7 (FAS_BOVIN)

Last modified October 13, 2009. Version 52. History...

Clusters with 100%, 90%, 50% identity |

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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 names

Recommended name:
    Fatty acid synthase
    EC=2.3.1.85
Including the following 7 domains:
    1- Recommended name:
            [Acyl-carrier-protein] S-acetyltransferase
              EC=2.3.1.38
    2- Recommended name:
            [Acyl-carrier-protein] S-malonyltransferase
              EC=2.3.1.39
    3- Recommended name:
            3-oxoacyl-[acyl-carrier-protein] synthase
              EC=2.3.1.41
    4- Recommended name:
            3-oxoacyl-[acyl-carrier-protein] reductase
              EC=1.1.1.100
    5- Recommended name:
            3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
              EC=4.2.1.61
    6- Recommended name:
            Enoyl-[acyl-carrier-protein] reductase
              EC=1.3.1.10
    7- Recommended name:
            Oleoyl-[acyl-carrier-protein] hydrolase
              EC=3.1.2.14

Gene names

Name:

FASN

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	2513 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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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. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.
Catalytic activity	Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) 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]. Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO₂ + [acyl-carrier-protein]. (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP⁺ = 3-oxoacyl-[acyl-carrier-protein] + NADPH. (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] = hexadec-2-enoyl-[acyl-carrier-protein] + H₂O. Acyl-[acyl-carrier-protein] + NADP⁺ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH. Oleoyl-[acyl-carrier-protein] + H₂O = [acyl-carrier-protein] + oleate.
Subunit structure	Homodimer which is arranged in a head to tail fashion By similarity.
Subcellular location	Cytoplasm By similarity. Melanosome By similarity.
Sequence similarities	Contains 1 acyl carrier domain.

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Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Ligand	NAD NADP Phosphopantetheine Pyridoxal phosphate
Molecular function	Hydrolase Lyase Oxidoreductase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Inferred from electronic annotation. Source: EC 3-oxoacyl-[acyl-carrier-protein] reductase activity Inferred from electronic annotation. Source: EC 3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: EC [acyl-carrier-protein] S-acetyltransferase activity Inferred from electronic annotation. Source: EC [acyl-carrier-protein] S-malonyltransferase activity Inferred from electronic annotation. Source: EC acyl carrier activity Inferred from electronic annotation. Source: InterPro cofactor binding Inferred from electronic annotation. Source: InterPro enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Inferred from electronic annotation. Source: EC oleoyl-[acyl-carrier-protein] hydrolase activity Inferred from electronic annotation. Source: EC phosphopantetheine binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2513

2513

Fatty acid synthase

PRO_0000180274

Regions

Domain

2125 – 2181

Acyl carrier

Nucleotide binding

1673 – 1690

NADP (ER) By similarity

Nucleotide binding

1888 – 1903

NADP (KR) By similarity

Region

1 – 414

414

Beta-ketoacyl synthase

Region

429 – 817

389

Acyl and malonyl transferases

Region

1637 – 1865

229

Enoyl reductase

Region

1866 – 2119

254

Beta-ketoacyl reductase

Region

2209 – 2513

305

Thioesterase

Sites

Active site

161

For beta-ketoacyl synthase activity By similarity

Active site

581

For malonyltransferase activity By similarity

Active site

878

For beta-hydroxyacyl dehydratase activity By similarity

Active site

2310

For thioesterase activity By similarity

Active site

2483

For thioesterase activity By similarity

Amino acid modifications

Modified residue

N-acetylmethionine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

207

Phosphoserine By similarity

Modified residue

298

N6-acetyllysine By similarity

Modified residue

528

N6-acetyllysine By similarity

Modified residue

673

N6-acetyllysine By similarity

Modified residue

1706

N6-(pyridoxal phosphate)lysine By similarity

Modified residue

1706

N6-acetyllysine By similarity

Modified residue

1754

N6-acetyllysine By similarity

Modified residue

1773

N6-acetyllysine By similarity

Modified residue

1849

N6-acetyllysine By similarity

Modified residue

1997

N6-acetyllysine By similarity

Modified residue

2158

O-(pantetheine 4'-phosphoryl)serine By similarity

Modified residue

2238

Phosphoserine By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q71SP7-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D75B09DB855DFDAB
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FASTA

2,513

274,554

        10         20         30         40         50         60 
MEEVVITGMS GKLPESENLE EFWANLIGGV DMVTDDDRRW KAGLYGLPRR SGKLKDLSRF 

        70         80         90        100        110        120 
DASFFGVHPK QAHNMDPQLR LLLEVTYEAI VDAGINPASI RGTNTGVWVG VSGSEASEAL 

       130        140        150        160        170        180 
SRDPETLVGY SMVGCQRAML ANRLSFFFDF KGPSITLDTA CSSSLLALQR AYQAIQRGEC 

       190        200        210        220        230        240 
AMAIVGGVNI RLKPNTSVQF MKLGMLSPEG TCKFFDASGN GYCRAKAVMA ILLTKKSLAR 

       250        260        270        280        290        300 
RVYATILNAG TNTDGCKEKG VTFPSGEAQE QLISSLYKPA GLDPETLEYV EAHGTGTKVG 

       310        320        330        340        350        360 
DPQELNGIVQ ALCGTRQSPL RIGSTKSNMG HPEPASGLAA LAKVLLSLEH GLWAPNLHFH 

       370        380        390        400        410        420 
NPNPKIPALQ DGRLQVVDRP LPVLGGNVGI NSFGFGGSNV HVILQPNSQP LPPPAPHAAL 

       430        440        450        460        470        480 
PRLLRASGRT LEGVQGLLEL GLQHSQNLAF VSMLNDIATP SPAAMPFRGY AVLGSQGGSQ 

       490        500        510        520        530        540 
KVQQVLAGKR PLWFICSGMG TQWRGMGLSL MRLSRFRDSI LRSDEAVKPL GLQVSQLLLS 

       550        560        570        580        590        600 
TDEAIFDDMV ISFVSLTAIQ IALIDLLTSM GLQPDGIIGH SLGEVACGYA DGCISQEEAI 

       610        620        630        640        650        660 
LSAYWRGQCI KEANIPPGAM AAVGLTWEEC KQRCPPGIVP ACHNCIDTVT ISGPQASMLE 

       670        680        690        700        710        720 
FVQQLKQEGV FAKEVRTGGM AFHSYFMDAI APMLLQQLKK VIREPQPRSP RWLSTSIPET 

       730        740        750        760        770        780 
QWQESLARTF SAEYNVNNLV SPVLFQEALW RVPEDAVVLE IAPHALLQAV LKRGLKSSCT 

       790        800        810        820        830        840 
IIPLMKKDHR DNLEFFLSNV GQLYLTGIDV NPNGLFPPVE FPAPRGTPLI SPHIKWDHSQ 

       850        860        870        880        890        900 
TWDVPTAEDF PSGSSSSSAT IYKIDINPES PDHYLVDHCI DGRIIFPGTG YLCLVWKTLA 

       910        920        930        940        950        960 
RALDQNMEHT PVVFEDVTLH QAVILPKTGI VLLKVRLLEA SCTFEVSENG NLIASGKVYQ 

       970        980        990       1000       1010       1020 
WEDPNPKLFD NRYGPDPATP VDPTTAIHLS RGDVYKELQL QGFNYGPYFQ GILEASSEGN 

      1030       1040       1050       1060       1070       1080 
TGQLLWKDNW VTFMDTMLQM SILAPSKRSL RLPTRITAIY IHPATHQQKL YTLQDKTQVA 

      1090       1100       1110       1120       1130       1140 
DVVINRCLDT TVAGGIYISR IHTSVAPRHQ QEQLVPILEK FCFTPHVETG CLAGNLALQE 

      1150       1160       1170       1180       1190       1200 
ELQLCVGLAQ ALQTRVAQQG IKMVVPGLDG AQAPQEAPQQ GLPRLLATAC QLQLNGNLQM 

      1210       1220       1230       1240       1250       1260 
EMGQILAQER ALLCDDPLLS GLLNSPALKA CVTLALENMT SLKMKVVLAG DGQLYSRIPT 

      1270       1280       1290       1300       1310       1320 
LLNTQPLLEL DYTATDRHPQ ALEAAQAKLQ QLDITQGQWD PSDPAPSNLG GANLVVCNYA 

      1330       1340       1350       1360       1370       1380 
LASLGDPATA VGNMVAALKE GGFLLLHTLL RGHPLGETVT FLTCPEPQQG QRHLLSQDEW 

      1390       1400       1410       1420       1430       1440 
ERLFAGASLH LVALKKSFYG SVLFLCRRLA PLDSPIFLPV EDTSFQWVDS LKNILADSSS 

      1450       1460       1470       1480       1490       1500 
RAVWLMAVGC TTSGVVGLVN CLRKEPDGHR IRCVLVSNLN STSPIPETDP KSLELQKVLQ 

      1510       1520       1530       1540       1550       1560 
SDLVMNVYRD GAWGAFRHFP LEQDKPEEQT EHAFINVLTR GDLSSIRWVC SPLRHSQPTA 

      1570       1580       1590       1600       1610       1620 
PGFQLCTIYY ASLNFKRNHA GHGQAVPRRH PRNWASRNCL LGMEFSGRDA SGKRVMGLVP 

      1630       1640       1650       1660       1670       1680 
AEGLATSTLV PQSFLWDVPS NWTLEEAASV PVVYSTAYYA LMVRGRMQPG ETVLIHSGSG 

      1690       1700       1710       1720       1730       1740 
GVGQAAIAIA LSLGCRVFPL VGSAEKRAYL QSRFPQLNET SFANSRDTSF EQHVLWHTAG 

      1750       1760       1770       1780       1790       1800 
KGADLVLNSL AEEKLQASVR CLAQHGRFLE IGKFDLSKNH PLGMAIFLKN VTFHGILLDS 

      1810       1820       1830       1840       1850       1860 
LFEENNTMWQ EVSTLLKAGI RKGVVQPLKR TVFPRTQAED AFRYMAQGKH IGKVVIQVRE 

      1870       1880       1890       1900       1910       1920 
EEQEAVLHGT KPTQMVALCK TFCPAHKSYI ITGGLGGFGL ELAHWLVERG AQKLVLTSRS 

      1930       1940       1950       1960       1970       1980 
GIRTGYQARQ VHEWRRQGVQ VLVSTSDVST LDGTRSLITE AAQLGPVGGI FNLAVVLRDA 

      1990       2000       2010       2020       2030       2040 
MLDNQTPEFF QDVNKPKYNG TLNLDRVTRE ACPELDYFEV FSSVSCGRGN AGQTNYGFAN 

      2050       2060       2070       2080       2090       2100 
STMERICEKR RHDGLPGLAV QWGAIADVGL LMELKGTKDK AIGGTLPQRI TSCMEVLDLF 

      2110       2120       2130       2140       2150       2160 
LNQPHPVLSS FVLAEKATSR GPSGSHQDLV KAVTHILGIR DLATVNLDSS LSDLGLDSLM 

      2170       2180       2190       2200       2210       2220 
GVEVRQMLER EHNLLLSMRE IRQLTIHKLQ EISAQAGTAD ELTDSTPKFG SPAQSHTQLN 

      2230       2240       2250       2260       2270       2280 
LSTLLVNPEG PTLTRLNSVQ SSERPLFLVH PIEGSTTVFH SLATKLSIPT YGLQCTGAAP 

      2290       2300       2310       2320       2330       2340 
LDSIQSLATY YIECIRQVQP EGNYRIAGYS YGACVAFEMC SQLQAQQNAG PTNNSLFLFD 

      2350       2360       2370       2380       2390       2400 
GSHTFVMAYT QSYRAKLNPG CEAEAEAEAM CFFMQQFTEA EHSRVLEALL PLGDLEARVA 

      2410       2420       2430       2440       2450       2460 
ATVELIVQSH AGLDRHALSF AARSFYHKLR AAEEYTPRAT YHGNVTLLRA KMGSAYQEGL 

      2470       2480       2490       2500       2510 
GADYNLSQVC DGKVSVHIIE GDHRTLLEGS GLESILSIIH SSLAEPRVSV REG

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References

[1]	"Cloning, genomic organization and expression analysis of bovine FASN gene." Roy R., Eggen A., Rodellar C. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

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Cross-references

Sequence databases
	AF285607 Genomic DNA. Translation: AAR19788.1. AY343889 mRNA. Translation: AAR17600.1.
IPI	IPI00712133.
RefSeq	NP_001012687.1.
UniGene	Bt.30099
3D structure databases
SMR	Q71SP7. Positions 2121-2196, 2219-2504.
ModBase	Search...
Protein-protein interaction databases
STRING	Q71SP7.
Genome annotation databases
GeneID	281152.
KEGG	bta:281152.
Organism-specific databases
CTD	281152.
Phylogenomic databases
HOVERGEN	Q71SP7.
Enzyme and pathway databases
BRENDA	1.1.1.100. 251. 1.3.1.10. 251. 2.3.1.38. 251. 2.3.1.39. 251. 2.3.1.41. 251. 2.3.1.85. 251. 3.1.2.14. 251. 4.2.1.61. 251.
Family and domain databases
InterPro	IPR001227. Ac_transferase_reg. IPR009081. Acyl_carrier_prot-like. IPR014043. Acyl_transferase. IPR013149. ADH_Zn-bd. IPR000794. Beta-ketoacyl_synthase. IPR002198. DH_sc/Rdtase_SDR. IPR018201. Ketoacyl_synth_AS. IPR014031. Ketoacyl_synth_C. IPR014030. Ketoacyl_synth_N. IPR013217. Methyltransf_12. IPR016040. NAD(P)-bd_dom. IPR006163. Phsphopanteth_bd. IPR006162. PPantetheine_attach_site. IPR001031. Thioesterase. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.366.10. Ac_transferase_reg. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 2 hits. G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
PANTHER	PTHR11712. Ketoacyl_synth. 1 hit.
Pfam	PF00698. Acyl_transf_1. 1 hit. PF00106. adh_short. 1 hit. PF00107. ADH_zinc_N. 1 hit. PF00109. ketoacyl-synt. 1 hit. PF02801. Ketoacyl-synt_C. 1 hit. PF08242. Methyltransf_12. 1 hit. PF00550. PP-binding. 1 hit. PF00975. Thioesterase. 1 hit. [Graphical view]
PROSITE	PS50075. ACP_DOMAIN. 1 hit. PS00606. B_KETOACYL_SYNTHASE. 1 hit. PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

FAS_BOVIN

Accession

Primary (citable) accession number: Q71SP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	July 5, 2004
Last modified:	October 13, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents