(data stored in ACNUC7421 zone)

SWISSPROT: Q757C8_ASHGO

ID   Q757C8_ASHGO            Unreviewed;      2046 AA.
AC   Q757C8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 111.
DE   RecName: Full=Fatty acid synthase subunit beta {ECO:0000256|PIRNR:PIRNR005562};
DE            EC=2.3.1.86 {ECO:0000256|PIRNR:PIRNR005562};
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase {ECO:0000256|PIRNR:PIRNR005562};
DE              EC=4.2.1.59 {ECO:0000256|PIRNR:PIRNR005562};
DE   Includes:
DE     RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|PIRNR:PIRNR005562};
DE              EC=1.3.1.9 {ECO:0000256|PIRNR:PIRNR005562};
DE   Includes:
DE     RecName: Full=[Acyl-carrier-protein] acetyltransferase {ECO:0000256|PIRNR:PIRNR005562};
DE              EC=2.3.1.38 {ECO:0000256|PIRNR:PIRNR005562};
DE   Includes:
DE     RecName: Full=[Acyl-carrier-protein] malonyltransferase {ECO:0000256|PIRNR:PIRNR005562};
DE              EC=2.3.1.39 {ECO:0000256|PIRNR:PIRNR005562};
DE   Includes:
DE     RecName: Full=S-acyl fatty acid synthase thioesterase {ECO:0000256|PIRNR:PIRNR005562};
DE              EC=3.1.2.14 {ECO:0000256|PIRNR:PIRNR005562};
GN   ORFNames=AGOS_AER085C {ECO:0000313|EMBL:AAS52769.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52769.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52769.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain
CC       fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit
CC       contains domains for: [acyl-carrier-protein] acetyltransferase and
CC       malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-
CC       [acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-
CC       protein] dehydratase. {ECO:0000256|PIRNR:PIRNR005562}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) +
CC         holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005562};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005562};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC         H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC         COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005562};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC         fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC         Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:83139; EC=2.3.1.86;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005562};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA;
CC         Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78446; EC=2.3.1.38;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005562};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005562};
CC   -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC       (alpha and beta). {ECO:0000256|PIRNR:PIRNR005562}.
CC   -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC       family. {ECO:0000256|PIRNR:PIRNR005562}.
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DR   EMBL; AE016818; AAS52769.2; -; Genomic_DNA.
DR   RefSeq; NP_984945.2; NM_210299.2.
DR   STRING; 33169.AAS52769; -.
DR   EnsemblFungi; AAS52769; AAS52769; AGOS_AER085C.
DR   GeneID; 4621149; -.
DR   KEGG; ago:AGOS_AER085C; -.
DR   HOGENOM; HOG000177963; -.
DR   InParanoid; Q757C8; -.
DR   KO; K00668; -.
DR   OMA; NVENQQY; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005835; C:fatty acid synthase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR   GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004319; F:enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity; IEA:EnsemblFungi.
DR   GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016409; F:palmitoyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:EnsemblFungi.
DR   Gene3D; 3.20.20.70; -; 2.
DR   Gene3D; 3.40.366.10; -; 2.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013565; DUF1729.
DR   InterPro; IPR041099; FAS1_N.
DR   InterPro; IPR040883; FAS_meander.
DR   InterPro; IPR003965; Fatty_acid_synthase.
DR   InterPro; IPR016452; Fatty_acid_Synthase_bsu_fun.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR039569; MaoC-like_dehydrat_N.
DR   InterPro; IPR002539; MaoC-like_dom.
DR   InterPro; IPR020801; PKS_acyl_transferase.
DR   InterPro; IPR032088; SAT.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08354; DUF1729; 1.
DR   Pfam; PF17951; FAS_meander; 1.
DR   Pfam; PF17828; FAS_N; 1.
DR   Pfam; PF13452; MaoC_dehydrat_N; 1.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   Pfam; PF16073; SAT; 1.
DR   PIRSF; PIRSF005562; FAS_yeast_beta; 1.
DR   PRINTS; PR01483; FASYNTHASE.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; SSF52151; 2.
DR   SUPFAM; SSF54637; SSF54637; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q757C8.
DR   SWISS-2DPAGE; Q757C8.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR005562};
KW   Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR005562};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR005562};
KW   Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR005562};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR005562};
KW   Lyase {ECO:0000256|PIRNR:PIRNR005562};
KW   Multifunctional enzyme {ECO:0000256|PIRNR:PIRNR005562};
KW   NAD {ECO:0000256|PIRNR:PIRNR005562}; NADP {ECO:0000256|PIRNR:PIRNR005562};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR005562};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|PIRNR:PIRNR005562, ECO:0000256|SAAS:SAAS01079871}.
FT   DOMAIN          1661..2014
FT                   /note="PKS_AT"
FT                   /evidence="ECO:0000259|SMART:SM00827"
FT   COILED          187..207
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        273
FT                   /note="For acetyltransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT   ACT_SITE        1804
FT                   /note="For malonyltransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ   SEQUENCE   2046 AA;  227741 MW;  76F64A0632EAA15B CRC64;
     MSGITTRSLA LGHGALEHTL SVPTGLYLTA SQLAASFAKE QVAPTEGYAS DEEPASSAEL
     LAKFVGHVAA QAGAGGEVAA VLELALDEFE ASYMCGEEVH RVAARLLADD EQPTALPKVK
     ELVQHYVYGS VRAQRPLMHR RPALLESATR GDARVVAVFG GQGNTDDYFE ELRELHQMYG
     VLVEDVLDTA AEQLNELLRT TEGAEKMYTQ GLDFRQWLAQ PERTPDNDYL LLIPISCPLI
     GILQLAHYAV TARIVGITPG ELRACMVGVT GHSQGLSTAV AVAEADTWES FFCALRKTVS
     LLFFIGVRCY QVYPKTSLPP SILEDSLENG EGKPSPMLSV SNLTQEQVQE FVEKTNAHLP
     SEKHIVISLV NGARNLVVSG PPQSLYGLNL ALRRAKAPAG LDQSRIPHSE RKLKFTNRFL
     PIESPFHSHL LEPALELIKQ DLHDADLEFK QESLAIAVYD TYDGHDLRQH SGSIVERIAS
     CITKLPVYWE TATTFKSTHI LDYGPGGASG LGVLTHRNKD GTGVRVIIAG ALDHNIDDEY
     GFKQELFDVN PTSLKFASNW LEEFHPKLIK TGSGKVYVDT KFSRLLGRPP LLVPGMTPTT
     VSPDFVAATI NSGYHIELAG GGYFSPQGMT EAIDSVVAQI KKGSSLGINL IYVNPRMLQW
     GIPLIKELRS KGYPIQSLTI GAGVPSLEVA SEYIETLGMT HLGLKPGSVD AISQVITIAK
     AHPTFPIVVQ WTAGRGGGHH SFENFHAPML QMYGKLRRHS NIILIAGSGF GSSEETYPYL
     TGEWSTRFNY PPMPFDGFLF GSRVMVAKEA KTSLAAKKAI AACTGVPDEL WEQTYKKPTG
     GIVTVRSEMG EPIHKIATRG VMLWKELDET IFNLPKNKLQ PALDAKRDYI IQKLNSDFQK
     PWFATVNGEA RELTDMTYKE VAERMVELMF IKSTGKWIDV TLRNFTGDFL RRVEERFTKD
     KSVSVLQSYS DLETPSKVLA DIFSAYPAAK SQFVNAQDVA YFLECAQRPT QKPVPFIPVL
     DHRFEFFFKK DSLWQSENLE AVVDEDVQRT CILHGPVAAQ YTKEINEPIQ HILDSIHDGH
     INKLLKDYYS DDISKVPVVE YFGGENPREV DYPTVKKTPD TIVYNATSAT DFRTWFNVLA
     GSQKSWRHAF FSIPRVVQGS RYSENPTFKV FKPCDNMVVT IKHPETPDKT EVILQEPVQG
     TLKTTATVTF SGDVIQLSMI ENRTMDGIPV ALPLLYKYNP TDGFAPIVEI MEDRNQRIKE
     MYWKLWLKDP FNLDFDPRDP IESEDFTITS KDIAAFTHAI GNNCEDFVTR PGRPLLAPMD
     FAIVIGWRAL VKAIFPNNVD GDLLNLVHLS NSYRMIPGAK PLQENDVVNV SALIKSVVNQ
     ENGKLVEVVG TIKKSGKPVI EVTTSFLYRG KYSDFENTFQ KSTDPVYVIQ INSPKDIAVL
     KSKEWLHFDN DKIDLLGRTL TFETETEVTF KNRTVFSSVH CEGRVLMELS TKENVQIGVV
     KYDAGESHGN PVIDYLSRNG STLEHKVNLE NTIPIATIEA QSPGTNETYA RVSGDLNPIH
     VSRHFANYAD LPGTITHGMY TSGAVRALVE TWAADSVSSR VRAYSCQFVG MVLPNTLLTT
     RIEHVGMING RKLIKFETRN DKDEPVLAGE AEVQQPVSTF VFTGQGSQEQ GMGMDLYDKS
     PVARQVWDRA DNHFKQTYGF SILEIVRTNP KELTIYFGGE KGRKIKENYT SMIFETIVDG
     EIASERIFKS ITESSTSYTF KSDTGLLSAT QFTQPALTLM EKASFEDLKS KGLIPAEATF
     AGHSLGEYAA LASLADVMSI ESLVEVVFYR GMTMQVAVPR DSEGRSNYGM IAVNPSRVST
     GFTQEALQFV VERVGKITEW LVEIVNYNVE DQQYVAAGDL RALDTLTNVL NFVKLQKIDL
     VKLQATMPLE QVEEHLDEII TEISKKSLSK PQPIELERGF ACIPLRGISV PFHSSYLRNG
     VKPFKNFLKK NIIKENVKVD RLIGKYIPNL TAKPFAITKE YFEDVYKLTG SEKIKAVLDN
     WESYQN
//

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