ID Q96WR1_LACKL Unreviewed; 2049 AA.
AC Q96WR1;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 84.
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 Name=Sk-FAS1 {ECO:0000313|EMBL:BAB62141.1};
OS Lachancea kluyveri (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4934 {ECO:0000313|EMBL:BAB62141.1};
RN [1] {ECO:0000313|EMBL:BAB62141.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO1893 {ECO:0000313|EMBL:BAB62141.1};
RX PubMed=11571758; DOI=10.1002/yea.785;
RA Kajiwara S., Oura T., Shishido K.;
RT "Cloning of a fatty acid synthase component FAS1 gene from Saccharomyces
RT kluyveri and its functional complementation of S. cerevisiae fas1 mutant.";
RL Yeast 18:1339-1345(2001).
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}.
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DR EMBL; AB054690; BAB62141.1; -; Genomic_DNA.
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; 3.30.70.2430; -; 1.
DR Gene3D; 6.10.140.1400; -; 1.
DR Gene3D; 6.10.250.1850; -; 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; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
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 1664..2017
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 275
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1807
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2049 AA; 228294 MW; 0828DCC11335B06E CRC64;
MSSSTRPLTL SHGSIEHVLP VPTASFFPAS QLQDQFSKQL PEVTEGFASD DEPASPAELL
GKFLGYVASL VDPTTKGPFD DVLQVSLGEF ESNFLQGNDV HTLAARLLAD DETNPTTLEK
VKELIKNYFN ARIVAQKPFA KSDSALFKSA AAKESKLVAI FGGQGNTDDY FEELRELYQT
YNSLISDVIK SAADRLAELV RSTDDTEKVY TQGFNIMEWL EHPEKTPDTD YLLSIPISCP
LIGVIQFVHY AVTARVLGFT PGELRSHLTG ATGHSQGLAT AVAIAEADSW ESFFQSLNKT
VALLFFIGVR CYQVYPNTSL PPSTLEDSVE NGEGTPSPML SISNLTKEQV QSFVDKTNAH
LPEEKHMRSF SLVNGARNLV VSGPPQSLYG LNLTLRKAKA PSGLDQARIP YSERKLKFSN
RFLPIASPFH SHLLEPANEL IKQDLVDAGV EFKQSDLKVP IFDTFSGKDM REQEGSIVER
ITYCITKLPV NWEITTQFES THILDFGPGG ASGLGVLTYR NKDGTGVRVI VAGALDNSPE
DEYGFKQEIF DVTANGLKFS PNWLEEFHPK LAKTKAGKVY VDTKFSRLLG RAPLLVPGMT
PTTVSPDFVA STINAGYHIE LAGGGYFSPD GMTKAIDSVV SQVKKGYGLG INLIYVNPRM
LQWGIPLIKE LRDKGYPIQS LTIGAGVPSL EVATEYIETL GLTHLGLKPG SIDAISQVIA
IAKAHPSFPI VMQWTGGRGG GHHSFEDFHA PMLQMYSKLR RHSNIILIAG SGFGSADDTY
PYLTGEWSAE FNYPPMPFDG FLFGSRVMIA KEAMTSPNAK KAIAACTGVP DSQWEQTYKK
PTGGIITVRS EMGEPIHKLA TRGVVFWKEM DDTIFNLPKN KLQAALDAKK DYIISKLNAD
YQKPWFATVN GEVRDLTDMT YEEVAKRMVE LMYIDSSKEW IDASLRNFTG DFLRRVEERF
TKKKTSSVLQ SYSLLDEPEK ALDIVFNAYP AAKEQFLNAQ DIDYFLTLCQ SPTQKPPPFV
PVLDHRFEFF FKKDSLWQSE HLEAVVDQDV QRTCILHGPV AAQFTNNVNE PIQSIMDGIH
NGHIEKLLKN YYAGDESKVP VVEYFGGEDP EDIKYDSVEA DGKITYRPSS TTDEATWFKL
LAGTERNWRH AFFSTSRVVQ GSLYDENPAK RVFKPSKNMV VQISHPKDAK KTVIKLLEQV
QGELKATASL QLVKDNLIEL QLIENRTIDG KPVALPLLYT YQPEDGFAPI AEVMEARNER
IKEMYWKLWL DEPLDLNFDP RKPLQGGEVK ITAKDIAEFT HAIGNNCEDF VARPGRKILA
PMDFAIVVGW RVIIKAIFPK AVDGDLLKLV HMSNGYRMMP GAKPLQEGDV ISSTAIIKSV
VNQPNGKVVN VVGTLSREDE PVMEVTSSFF YRGKYDDFEN TFQKTTEPTY QVNIKSAKDI
AVLRSKEWFQ LDDEDIDLLG KTLTFETETE VTFKNETVFN SVKCEGKILM ELPTKETIEI
GVVDYEAGES HGNPVTDYLS RNGSTLEQKV NLENAIPIAV RESQAPGTNE PYARVSGDLN
PIHVSRHFAS YAKLPGTITH GMYSSAAVRA LVETWAADNV SSRVRAYDCQ FVGMVLPNTP
LKTSIQHVGM INGRKLIKFE TKNDQEETVL IGEAEVEQPV STFVFTGQGS QEQGMGMDLY
GKSEVAKQVW DRADIHFKET YGFSILDIVK NNPTEMTIYF GGEKGRKIKE NYTQMIFETI
VDGKLKTEKI FKDITEETTS YTFMSPTGLL SATQFTQPAL TLMEKASFED LKSKGLIPVD
AAFAGHSLGE YAALASLADV MSIESLVEVV FYRGMTMQVA VPRDDLGRSN YGMVAVNPGR
VSPTFSQEAL QFVVECVGKR TEWLVEIVNY NVENQQYVAA GDLRALDSLT NVLNFIKLQK
VDIAKLQSSM SLEEVGGHLN EIIDEVSKKS TAKEQPIELE RGFATIPLRG ISVPFHSSYL
RNGVKPFKNF LMKNIIKENV KADRLIGKYI PNLTAKPFQI TKEYFQDVYD LTGSEKIKDI
LDNWEKYQN
//
