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P34731

- FAS1_CANAX

UniProt

P34731 - FAS1_CANAX

Protein

Fatty acid synthase subunit beta

Gene

FAS1

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    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 sitei261 – 2611For acetyltransferase activityBy similarity
    Active sitei1796 – 17961For 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
    OrganismiCandida albicans (Yeast)
    Taxonomic identifieri5476 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    Subcellular locationi

    GO - Cellular componenti

    1. fatty acid synthase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20372037Fatty acid synthase subunit betaPRO_0000180280Add
    BLAST

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP34731.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1506 – 1634129MaoC-likeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 453453AcetyltransferaseBy similarityAdd
    BLAST
    Regioni465 – 798334Enoyl reductaseBy similarityAdd
    BLAST
    Regioni1132 – 1612481DehydrataseBy similarityAdd
    BLAST
    Regioni1613 – 1833221Malonyl/palmitoyl transferaseBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 MaoC-like domain.Curated

    Phylogenomic databases

    eggNOGiCOG0331.

    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.

    P34731-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTHRPFQLT HGSIEHTLLV PNDLFFNYSQ LKDEFIKTLP EPTEGFAGDD     50
    EPSSPAELYG KFIGFISNAQ FPQIVELSLK DFESRFLDNN NDNIHSFAVK 100
    LLDDETYPTT IAKVKENIVK NYYKAVKSIN KVESNLLYHC KHDAKLVAIF 150
    GGQGNTDDYF EELRELYTLY QGLIEDLLVS IAEKLNQLHP SFDKIYTQGL 200
    NILSWLKHPE TTPDQDYLLS VPVSCPVICV IQLCHYTITC KVLGLTPGEF 250
    RNSLKWSTGH SQGLVTAVTI AASDSWDSFL KNSLTAVSLL LFIGSRCLST 300
    YPRTSLPPTM LQDSLDNGEG RPSPMLSVRD LSIKQVEKFI EQTNSHLPRE 350
    KHIAISLING ARNLVLSGPP ESLYGFNLNL RNQKAPMGLD QSRVPFSERK 400
    LKCSNRFLPI FAPFHSHLLA DATELILDDV KEHGLSFEGL KIPVYDTFDG 450
    SDFQALKEPI IDRVVKLITE LPVHWEEATN HKATHILDFG PGGVSGLGVL 500
    THRNKEGTGA RIILAGTLDS NPIDDEYGFK HEIFQTSADK AIKWAPDWLK 550
    ELRPTLVKNS EGKIYVKTKF SQLLGRAPLM VAGMTPTTVN TDIVSASLNA 600
    GYHIELAGGG YFSPVMMTRA IDDIVSRIKP GYGLGINLIY VNPFMLQWGI 650
    PLIKDLREKG YPIQSLTIGA GVPSIEVATE YIEDLGLTHL GLKPGSVDAI 700
    SQVIAIAKAH PTFPIVLQWT GGRGGGHHSF EDFHQPIIQM YSKIRRCSNI 750
    VLVAGSGFGS DEDTYPYLSG YWSEKFNYPP MPFDGVLFGS RVMTSKESHT 800
    SLAAKKLIVE CKGVPDQQWE QTYKKPTGGI ITVRSEMGEP IHKIATRGVM 850
    FWKELDDTIF NLPKNKLLDA LNKKRDHIIK KLNNDFQKPW FGKNANGVCD 900
    LQEMTYKEVA NRLVELMYVK KSHRWIDVSL RNMYGDFLRR VEERFTSSAG 950
    TVSLLQNFNQ LNEPEQFTAD FFEKFPQAGK QLISEEDCDY FLMLAARPGQ 1000
    KPVPFVPVLD ERFEFFFKKD SLWQSEDLES VVDEDVQRTC ILHGPVASQY 1050
    TSKVDEPIGD ILNSIHEGHI ARLIKEEYAG DESKIPVVEY FGGKKPASVS 1100
    ATSVNIIDGN QVVYEIDSEL PNKQEWLDLL AGTELNWLQA FISTDRIVQG 1150
    SKHVSNPLHD ILTPAKHSKV TIDKKTKKLT AFENIKGDLL PVVEIELVKP 1200
    NTIQLSLIEH RTADTNPVAL PFLYKYNPAD GFAPILEIME DRNERIKEFY 1250
    WKLWFGSSVP YSNDINVEKA ILGDEITISS QTISEFTHAI GNKCDAFVDR 1300
    PGKATLAPMD FAIVIGWKAI IKAIFPKSVD GDLLKLVHLS NGYKMITGAA 1350
    PLKKGDVVST KAEIKAVLNQ PSGKLVEVVG TIYREGKPVM EVTSQFLYRG 1400
    EYNDYCNTFQ KVTETPVQVA FKSAKDLAVL RSKEWFHLEK DVQFDVLTFR 1450
    CESTYKFKSA NVYSSIKTTG QVLLELPTKE VIQVGSVDYE AGTSYGNPVT 1500
    DYLSRNGKTI EESVIFENAI PLSSGEELTS KAPGTNEPYA IVSGDYNPIH 1550
    VSRVFAAYAK LPGTITHGMY SSASIRALVE EWAANNVAAR VRAFKCDFVG 1600
    MVLPNDTLQT TMEHVGMING RKIIKVETRN VETELPVLIG EAEIEQPTTT 1650
    YVFTGQGSQE QGMGMELYNS SEVAREVWDK ADRHFVNNYG FSILDIVQNN 1700
    PNELTIHFGG AKGRAIRDNY IGMMFETIGE DGALKSEKIF KDIDETTTSY 1750
    TFVSPTGLLS ATQFTQPALT LMEKAAYEDI KSKGLIPSDI MFAGHSLGEY 1800
    SALSSLANVM PIESLVDVVF YRGMTMQVAV PRDELGRSNY GMVAVNPSRV 1850
    SATFDDSALR FVVDEVANKT KWLLEIVNYN VENQQYVAAG DLRALDTLTN 1900
    VLNVLKINKI DIVKLQEQMS IEKVKEHLYE IVDEVAAKSL AKPQPIDLER 1950
    GFAVIPLKGI SVPFHSSYLM SGVKPFQRFL CKKIPKSSVK PQDLIGKYIP 2000
    NLTAKPFELT KEYFQSVYDL TKSEKIKSIL DNWEQYE 2037
    Length:2,037
    Mass (Da):227,919
    Last modified:February 1, 1994 - v1
    Checksum:iD37BDD0DB9A8ADDA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74952 Genomic DNA. Translation: CAA52907.1.
    PIRiS37178.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74952 Genomic DNA. Translation: CAA52907.1 .
    PIRi S37178.

    3D structure databases

    ProteinModelPortali P34731.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0331.

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

    Entry informationi

    Entry nameiFAS1_CANAX
    AccessioniPrimary (citable) accession number: P34731
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3