Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P34229

- FAS1_YARLI

UniProt

P34229 - FAS1_YARLI

Protein

Fatty acid synthase subunit beta

Gene

FAS1

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (11 Oct 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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 activityi

    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 + an [acyl-carrier-protein] = CoA + a 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei286 – 2861For acetyltransferase activityBy similarity
    Active sitei1842 – 18421For malonyltransferase activityBy similarity

    GO - Molecular functioni

    1. [acyl-carrier-protein] S-acetyltransferase activity Source: UniProtKB-EC
    2. [acyl-carrier-protein] S-malonyltransferase activity Source: UniProtKB-EC
    3. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
    4. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB-EC
    5. fatty-acyl-CoA synthase activity Source: UniProtKB-EC
    6. myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
    7. oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
    8. palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Lyase, Oxidoreductase, Transferase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    NAD, NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid synthase subunit beta (EC:2.3.1.86)
    Including the following 5 domains:
    3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.59)
    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 namesi
    Name:FAS1
    Ordered Locus Names:YALI0B15059g
    OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
    Taxonomic identifieri284591 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
    ProteomesiUP000001300: Chromosome B

    Subcellular locationi

    GO - Cellular componenti

    1. fatty acid synthase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20862086Fatty acid synthase subunit betaPRO_0000180283Add
    BLAST

    Interactioni

    Subunit structurei

    [Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).

    Protein-protein interaction databases

    STRINGi4952.P34229.

    Structurei

    3D structure databases

    ProteinModelPortaliP34229.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1550 – 1680131MaoC-likeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 480480AcetyltransferaseAdd
    BLAST
    Regioni492 – 879388Enoyl reductaseAdd
    BLAST
    Regioni1166 – 1657492DehydrataseAdd
    BLAST
    Regioni1658 – 1879222Malonyl/palmitoyl transferaseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 MaoC-like domain.Curated

    Phylogenomic databases

    eggNOGiCOG0331.
    HOGENOMiHOG000177963.
    KOiK00668.
    OMAiKLQHVGM.
    OrthoDBiEOG76QFRJ.

    Family and domain databases

    Gene3Di3.10.129.10. 2 hits.
    3.20.20.70. 1 hit.
    3.40.366.10. 5 hits.
    InterProiIPR001227. 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.
    IPR029069. HotDog_dom.
    IPR002539. MaoC_dom.
    [Graphical view]
    PfamiPF00698. Acyl_transf_1. 1 hit.
    PF08354. DUF1729. 1 hit.
    PF01575. MaoC_dehydratas. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005562. FAS_yeast_beta. 1 hit.
    PRINTSiPR01483. FASYNTHASE.
    SUPFAMiSSF52151. SSF52151. 5 hits.
    SSF54637. SSF54637. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    P34229-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYPTTGVNTP QSAASLRPLV LSHGQTEHSL LVPTSLYINC TTLRDQFYAS     50
    LPPATEDKAD DDEPSSSTEL LAAFLGFTAK TVEEEPGPYD DVLSLVLNEF 100
    ETRYLRGNDI HAVASSLLQD EDVPTTVGKI KRVIRAYYAA RIACNRPIKA 150
    HSSALFRAAS EDSDNVSLYA IFGGQGNTED YFEELREIYD IYQGLVGDFI 200
    RECGAQLLAL SRDHIAAEKI YTKGFDIVKW LEHPETIPDF EYLISAPISV 250
    PIIGVIQLAH YAVTCRVLGL NPGQVRDNLK GATGHSQGLI TAIAISASDS 300
    WDEFYNSASR ILKIFFFIGV RVQQAYPSTF LPPSTLEDSV KQGEGKPTPM 350
    LSIRDLSLNQ VQEFVDATNL HLPEDKQIVV SLINGPRNVV VTGPPQSLYG 400
    LCLVLRKQKA ETGLDQSRVP HSQRKLKFTH RFLPITSPFH SYLLEKSTDL 450
    IINDLESSGV EFVSSELKVP VYDTFDGSVL SQLPKGIVSR LVNLITHLPV 500
    KWEKATQFQA SHIVDFGPGG ASGLGLLTHK NKDGTGVRTI LAGVIDQPLE 550
    FGFKQELFDR QESSIVFAQN WAKEFSPKLV KISSTNEVYV DTKFSRLTGR 600
    APIMVAGMTP TTVNPKFVAA TMNSGYHIEL GGGGYFAPGM MTKALEHIEK 650
    NTPPGSGITI NLIYVNPRLI QWGIPLIQEL RQKGFPIEGL TIGAGVPSLE 700
    VANEWIQDLG VKHIAFKPGS IEAISSVIRI AKANPDFPII LQWTGGRGGG 750
    HHSFEDFHAP ILQMYSKIRR CSNIVLIAGS GFGASTDSYP YLTGSWSRDF 800
    DYPPMPFDGI LVGSRVMVAK EAFTSLGAKQ LIVDSPGVED SEWEKTYDKP 850
    TGGVITVLSE MGEPIHKLAT RGVLFWHEMD KTVFSLPKKK RLEVLKSKRA 900
    YIIKRLNDDF QKTWFAKNAQ GQVCDLEDLT YAEVIQRLVD LMYVKKESRW 950
    IDVTLRNLAG TFIRRVEERF STETGASSVL QSFSELDSEP EKVVERVFEL 1000
    FPASTTQIIN AQDKDHFLML CLNPMQKPVP FIPVLDDNFE FFFKKDSLWQ 1050
    CEDLAAVVDE DVGRICILQG PVAVKHSKIV NEPVKEILDS MHEGHIKQLL 1100
    EDGEYAGNMA NIPQVECFGG KPAQNFGDVA LDSVMVLDDL NKTVFKIETG 1150
    TSALPSAADW FSLLAGDKNS WRQVFLSTDT IVQTTKMISN PLHRLLEPIA 1200
    GLQVEIEHPD EPENTVISAF EPINGKVTKV LELRKGAGDV ISLQLIEARG 1250
    VDRVPVALPL EFKYQPQIGY APIVEVMTDR NTRIKEFYWK LWFGQDSKFE 1300
    IDTDITEEII GDDVTISGKA IADFVHAVGN KGEAFVGRST SAGTVFAPMD 1350
    FAIVLGWKAI IKAIFPRAID ADILRLVHLS NGFKMMPGAD PLQMGDVVSA 1400
    TAKIDTVKNS ATGKTVAVRG LLTRDGKPVM EVVSEFFYRG EFSDFQNTFE 1450
    RREEVPMQLT LKDAKAVAIL CSKEWFEYNG DDTKDLEGKT IVFRNSSFIK 1500
    YKNETVFSSV HTTGKVLMEL PSKEVIEIAT VNYQAGESHG NPVIDYLERN 1550
    GTTIEQPVEF EKPIPLSKAD DLLSFKAPSS NEPYAGVSGD YNPIHVSRAF 1600
    ASYASLPGTI THGMYSSAAV RSLIEVWAAE NNVSRVRAFS CQFQGMVLPN 1650
    DEIVTRLEHV GMINGRKIIK VTSTNRETEA VVLSGEAEVE QPISTFVFTG 1700
    QGSQEQGMGM DLYASSEVAK KVWDKADEHF LQNYGFSIIK IVVENPKELD 1750
    IHFGGPKGKK IRDNYISMMF ETIDEKTGNL ISEKIFKEID ETTDSFTFKS 1800
    PTGLLSATQF TQPALTLMEK ASFEDMKAKG LVPVDATFAG HSLGEYSALA 1850
    SLGDVMPIES LVDVVFYRGM TMQVAVPRDA QGRSNYGMCA VNPSRISTTF 1900
    NDAALRFVVD HISEQTKWLL EIVNYNVENS QYVTAGDLRA LDTLTNVLNV 1950
    LKLEKINIDK LLESLPLEKV KEHLSEIVTE VAKKSVAKPQ PIELERGFAV 2000
    IPLKGISVPF HSSYLRNGVK PFQNFLVKKV PKNAVKPANL IGKYIPNLTA 2050
    KPFEITKEYF EEVYKLTGSE KVKSIINNWE SYESKQ 2086
    Length:2,086
    Mass (Da):231,342
    Last modified:October 11, 2004 - v2
    Checksum:i060F6CEA44F235B2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 1111MYPTTGVNTPQ → M in CAA42211. (PubMed:2034224)CuratedAdd
    BLAST
    Sequence conflicti529 – 5302HK → TR in CAA42211. (PubMed:2034224)Curated
    Sequence conflicti1240 – 12401V → G in CAA42211. (PubMed:2034224)Curated
    Sequence conflicti1612 – 16121H → Q in CAA42211. (PubMed:2034224)Curated
    Sequence conflicti2077 – 20771N → D in CAA42211. (PubMed:2034224)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59690 Genomic DNA. Translation: CAA42211.1.
    CR382128 Genomic DNA. Translation: CAG83163.1.
    PIRiS15999.
    RefSeqiXP_500912.1. XM_500912.1.

    Genome annotation databases

    EnsemblFungiiCAG83163; CAG83163; YALI0_B15059g.
    GeneIDi2907339.
    KEGGiyli:YALI0B15059g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59690 Genomic DNA. Translation: CAA42211.1 .
    CR382128 Genomic DNA. Translation: CAG83163.1 .
    PIRi S15999.
    RefSeqi XP_500912.1. XM_500912.1.

    3D structure databases

    ProteinModelPortali P34229.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 4952.P34229.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CAG83163 ; CAG83163 ; YALI0_B15059g .
    GeneIDi 2907339.
    KEGGi yli:YALI0B15059g.

    Phylogenomic databases

    eggNOGi COG0331.
    HOGENOMi HOG000177963.
    KOi K00668.
    OMAi KLQHVGM.
    OrthoDBi EOG76QFRJ.

    Family and domain databases

    Gene3Di 3.10.129.10. 2 hits.
    3.20.20.70. 1 hit.
    3.40.366.10. 5 hits.
    InterProi IPR001227. 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.
    IPR029069. HotDog_dom.
    IPR002539. MaoC_dom.
    [Graphical view ]
    Pfami PF00698. Acyl_transf_1. 1 hit.
    PF08354. DUF1729. 1 hit.
    PF01575. MaoC_dehydratas. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005562. FAS_yeast_beta. 1 hit.
    PRINTSi PR01483. FASYNTHASE.
    SUPFAMi SSF52151. SSF52151. 5 hits.
    SSF54637. SSF54637. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "The pentafunctional FAS1 genes of Saccharomyces cerevisiae and Yarrowia lipolytica are co-linear and considerably longer than previously estimated."
      Koettig H., Rottner G., Beck K.-F., Schweizer M., Schweizer E.
      Mol. Gen. Genet. 226:310-314(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 32338 / CX-161-1B.
    2. "Genome evolution in yeasts."
      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.
      Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CLIB 122 / E 150.

    Entry informationi

    Entry nameiFAS1_YARLI
    AccessioniPrimary (citable) accession number: P34229
    Secondary accession number(s): Q6CEK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3