ID A0A1E5RWF8_9ASCO Unreviewed; 2055 AA.
AC A0A1E5RWF8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AWRI3578_g473 {ECO:0000313|EMBL:OEJ91176.1};
OS Hanseniaspora opuntiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=211096 {ECO:0000313|EMBL:OEJ91176.1, ECO:0000313|Proteomes:UP000095605};
RN [1] {ECO:0000313|Proteomes:UP000095605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3578 {ECO:0000313|Proteomes:UP000095605};
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(2016).
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|ARBA:ARBA00001214,
CC 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|ARBA:ARBA00001055,
CC 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|ARBA:ARBA00000175,
CC 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|ARBA:ARBA00000343,
CC 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|ARBA:ARBA00001540,
CC 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|ARBA:ARBA00000936,
CC 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|ARBA:ARBA00010009, ECO:0000256|PIRNR:PIRNR005562}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEJ91176.1}.
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DR EMBL; LPNL01000002; OEJ91176.1; -; Genomic_DNA.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000095605; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:(3R)-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro.
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:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:RHEA.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03447; FAS_MaoC; 1.
DR Gene3D; 1.20.1050.120; -; 1.
DR Gene3D; 1.20.930.70; -; 1.
DR Gene3D; 3.30.1120.100; -; 1.
DR Gene3D; 3.30.70.3330; -; 1.
DR Gene3D; 6.10.140.1400; -; 1.
DR Gene3D; 6.10.60.10; -; 1.
DR Gene3D; 6.20.240.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
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; IPR016452; Fas1/AflB-like.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR041099; FAS1_N.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR039569; MaoC-like_dehydrat_N.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR032088; SAT.
DR PANTHER; PTHR10982:SF21; FATTY ACID SYNTHASE SUBUNIT BETA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; Fas1-AflB-like_hel; 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; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR005562};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832,
KW ECO:0000256|PIRNR:PIRNR005562};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005562};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR005562};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR005562};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR005562};
KW Multifunctional enzyme {ECO:0000256|PIRNR:PIRNR005562};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR005562};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR005562};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR005562};
KW Transferase {ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1671..1994
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 280
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1814
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2055 AA; 228710 MW; DE6185563D724C36 CRC64;
MSSNRLLTLQ YESVEHSFNV STDSYLVASQ LKEQFTKDVL PAAIDRTSEL AGDLEPQTTA
ELLGKFIGYA STFYSNQDSK PIENDYFSNI LKNAINDFES TFLQNSTVDI HSFVASLIEN
DSTTLQKGQE IIKNYLLGKV TIDGKFSGVQ STLIKNADKL DINAIFGGQG NTDDYFDELR
DLVSTYDVIM RDLLTFIDET IKELSNKIQN FDKIYTQGFD ILKWINQPEQ TPNTDYLLSI
PVSCPVIGII QLLNFAITCR LLGLNPGQLR SALRGATGHS QGLVTAIAIA ESNDWESFFK
AAKKGISLLF FIGCRCNESY PNTALSPSIS EDSVENGEGV PSPMLSISNL TKDQVQDYVD
KTNSHLPKEK HVVISLVNGA RNLVVSGPPQ SLYGLNLSLR KLKVASGLDQ NRIPHSQRKL
KFTNRFLPVT SPFHSHLLEP AMEAIEKDIL ENDITFKSSS LMIPVYDTFT GDDLAKTNSE
NLSSRLALLI VKHPVNWEVA TNFPACSHIL DFGPGGSSGL GVLTHRNKEG TGVRVILAGA
FDVSADDEYG FKQEIFNIKE DGLKLADNWV KDYSPKLVQT KSGKVFVETK FSKLISRAPL
LVPGMTPTTV SPXFVASTIN AGYHIELAGG GYFSPAMMTK AIDNIVSQIK PGFSLGLNLI
YVNPFMLQWG IPLIKELRSK GYPIQSLTIG AGVPSLEVAT EYIETLGLKH LGLKPGSVDA
ISQVINIAKA HPNFPIVLQW TGGRGGGHHS FEDFHQPILQ MYSKIRKYSN IHLIAGSGFG
SAEDTYPYLT GEWSKKFNYP PMPFDGFLFG SRVMIAKEAK TSPDAKLAIA KCSGVADSEW
ESTYQKPTGG ILTVKSEMGE PIHKIATRGV KFWKEMDDTI FSLPKNKLEX TLEAKKDYII
SKLNADFQKP WFATVNGVAK NIQDMTYAEV ADRLVELIFI KSTGKWIDVS LRNMTGDFLR
RIEERFTKTK TTSVLQSYSS LDTEPTKVLE AIFAKYPDSK VQFLNAQDVD FFLGLTTRRA
QKPVPFVPIL DKNFEFYFKK DSLWQSENLE TVIDQDVERT CILHGPVAAQ FTNKVDQPIK
EIMDEIHDGH ISKLLKDYYN NDKSSIPVVE YFGNDDAKVV EFPHTASESG VRRYTCNGST
NVSDWFNLLA GSKKNWRHAF FTTDHVVQGK FFESNPVKKI FAPVQGSEFV VEIDGEGAQS
KVTLFEKVAG SLTATASLRL NADGVVEFDL IESRTVDSKP VALTLLFNYH PEDGYSPIHE
VMEGRNDRIK EMYWKLWLPG KVDLNFDVHA PIDGGSVKVE TSDILNFTHA IGNNCEDFVP
RTGRKVLAPM DFAIVLGWRS IIKAIFPKSV DGDLLKLVHM SNGYKMIPGA KPIQEGDVVS
TTALVKSVVN QPNGKVVEVV GTLSRDSKPV MEVSSKFFYR GAYSDFENTF ERIAEVPYKL
NLNSAKDVAV LQSKEWFNLD SEVELLGKTL YFKLQTDVTY KSADVFSSVT SEGNVFYELP
TKELVKIGEV NYEAGQSHGN PVIDYLARNG TTTEEKVAFE NEIPITVQQT QSPSTNESYA
RVSGDLNPIH VSRHFAEYAN LPGTITHGMF SSASVRSLVE TWAADNVSSR VRGYKCDFTG
MVLPNTQLTT SIKHVGMING RKLIKFETKN SNEETVLVGE AEVEQPASTF VFTGQGSQEQ
GMGMDLYAKS EVARNVWDRA DNHFKETYGF SILEIVKKNP NELTIFFGGE KGKKIKENYT
SMMFETIVDG ELKSEKIFKD IVDTTTSYTF QSPTGLLSAT QFTQPALTLM EKAAFEDLKA
KGLIPNDAPF AGHSLGEYAA LASLADVMSI ESLVEVVFYR GMTMQVAVPR DSLGRSNYGM
IAVNPSRVHP SFSQEALQFV VQSVSKKTGW LLEIVNYNVE NQQYVAAGDL RALDTLGNVL
NVFKLQKINF VKLQESMTIE ELTEHLNEIT AEVSAKSVAK PQPIDLERGF ATIPLKGISV
PFHSSYLMSG VKPFKNFLKK NIVKENVKAD RLIGKYIPNL TAKPFELTKE YFEDVYQITK
SEKIKEIIEN WENYQ
//
