ID A0A6A6U0X3_9PEZI Unreviewed; 2089 AA.
AC A0A6A6U0X3;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=Fatty acid synthase subunit beta {ECO:0000256|ARBA:ARBA00068309};
DE EC=1.3.1.9 {ECO:0000256|ARBA:ARBA00012996};
DE EC=2.3.1.38 {ECO:0000256|ARBA:ARBA00013256};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
DE EC=2.3.1.86 {ECO:0000256|ARBA:ARBA00012878};
DE EC=3.1.2.14 {ECO:0000256|ARBA:ARBA00012480};
DE EC=4.2.1.59 {ECO:0000256|ARBA:ARBA00013167};
DE AltName: Full=S-acyl fatty acid synthase thioesterase {ECO:0000256|ARBA:ARBA00078671};
GN ORFNames=BT63DRAFT_482659 {ECO:0000313|EMBL:KAF2665752.1};
OS Microthyrium microscopicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Microthyriales; Microthyriaceae;
OC Microthyrium.
OX NCBI_TaxID=703497 {ECO:0000313|EMBL:KAF2665752.1, ECO:0000313|Proteomes:UP000799302};
RN [1] {ECO:0000313|EMBL:KAF2665752.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 115976 {ECO:0000313|EMBL:KAF2665752.1};
RA Haridas S., Albert R., Binder M., Bloem J., Labutti K., Salamov A.,
RA Andreopoulos B., Baker S., Barry K., Bills G., Bluhm B., Cannon C.,
RA Castanera R., Culley D., Daum C., Ezra D., Gonzalez J., Henrissat B.,
RA Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA Yoshinaga Y., Zwiers L.-H., Turgeon B., Goodwin S., Spatafora J., Crous P.,
RA Grigoriev I.;
RT "101 Dothideomycetes genomes: a test case for predicting lifestyles and
RT emergence of pathogens.";
RL Stud. Mycol. 0:0-0(2020).
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|ARBA:ARBA00058855}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + holo-
CC [ACP] + H(+); 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:ARBA00048536};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC NADH + H(+); 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:ARBA00048572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H(+) = a long-
CC chain-acyl-CoA + n CoA + n CO2 + 2n NADP(+).; EC=2.3.1.86;
CC Evidence={ECO:0000256|ARBA:ARBA00048237};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + acetyl-CoA = 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:ARBA00048835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA;
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:ARBA00048462};
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000256|ARBA:ARBA00033756}.
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; MU004240; KAF2665752.1; -; Genomic_DNA.
DR OrthoDB; 5417908at2759; -.
DR Proteomes; UP000799302; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0019171; F:(3R)-hydroxyacyl-[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:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0016297; F:fatty acyl-[ACP] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03447; FAS_MaoC; 1.
DR FunFam; 1.20.1050.120:FF:000001; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 1.20.930.70:FF:000001; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.10.129.10:FF:000017; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.20.20.70:FF:000078; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.30.1120.100:FF:000001; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.40.366.10:FF:000006; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.40.366.10:FF:000007; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.10.129.10:FF:000015; Fatty acid synthase subunit beta; 1.
DR FunFam; 3.20.20.70:FF:000169; Fatty acid synthase subunit beta; 1.
DR FunFam; 3.30.70.3330:FF:000001; Fatty acid synthase subunit beta dehydratase; 1.
DR FunFam; 3.40.366.10:FF:000003; Fatty acid synthase subunit beta dehydratase; 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; 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_dom.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR039569; FAS1-like_DH_region.
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; IPR050830; Fungal_FAS.
DR InterPro; IPR029069; HotDog_dom_sf.
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; PF13452; FAS1_DH_region; 1.
DR Pfam; PF22235; FAS1_thioest_ins; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF17828; FAS_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|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005562};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
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 Reference proteome {ECO:0000313|Proteomes:UP000799302};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1692..1992
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 284
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1836
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2089 AA; 232236 MW; E1B77AA05B50A759 CRC64;
MYGGSGAQTG INTPRTAASF RPLILSHGSL EHTFHITSDL HFTAVRLKDD FVATLPEPTD
ELALDDEPSS TAELVARYLG FIANEVKEAA EDIPTLTHLL VVLVTEFERV FLQGNDIHAV
SASLPGIPSK KLITVESYYN ARKSANRPLK TYESALFREA KDGNAGLYAI FGGQGNIEEY
FEELREIYTT YSIFVEDFIR ESAAHLLSLS LNEQAKKSYS KGLDVVRWLH NKDAQPDVDY
LVSAPVSLPL IGLTQLAHYM VTCKTLGVDP GYVRSLLKGT TGHSQGVVTA AAIATAHDWP
SFTKAAKDAI TILFWIGCRS QQVYPRTSIQ PNVIQDSIEN GEGDPTPMLS IRDLTLSTVQ
TYIDQTNEHL ADDKQIAISL VNSARNVVVT GPMLSLYGLN LTLRKVKAPT GLDQGRVPHS
QRKIRFTNRF LPITAPFHSP YLAETARLLE EDLKDITIPA KSLGIAMYHT DTGKDIRDDG
ASNIVPTLVQ MITRDPVNWE KATVFPNATH IIDFGPGGIS GLGVLTNRNK DGSGVRVILA
GSIDGTNAEV GYKPELFDRD QETAVKYAAD WVKEHGPKLV KTSSGRTYVD TKFSRLLGLP
PIMVAGMTPC TVAPEFIADT MNAGYEIELA GGGYFIRPMM TDAIKKVEAH IPPGRGISIN
LIYVNPRAMS WQVPMIGDLR AEGIPIVNMT IGAGVPSLEV ANEYIETLGL KRMAFKPGSL
DAIQAVVNIA RANPTFPVVL QWTGGRGGGH HSFEDFHQPI LTMYSRIRKC PNLVLVAGSG
FGGAEDTYPY LTGAWSAKYG YPPMPFDGCL FGSRMMVAKE AWTSPAAKQA IVDAPGVEDV
EWERTYTEPT GGVLTVLSEM GEPIHKLATR GVRFWAEMDQ KIFKLDKAKR VPELKKNRDY
IIKHLNEDFQ KPWFGKNSSG PCDLEEMTYG EIVRRCVELM YIKHQSRWVD VSLRAFTVTI
FRRVEERFAT SSGAKSVVQN PNDLNDPFPI IDKLLAAYPE AEKQLISAQD VQFFLQCCMN
PLQKPVTFVP CFDDNFDFYF KKDSLWQSED VEAVMDQDVQ RVCILQGPMA AKYSTKVDEP
IKDILDGIHE GHIKMLLKDL YNNDESKIPV TDYFGGKLVE ASDERHSLDG LTVKEEADKL
TFKLSAAPNA TLPQLDNWLE LLAGKTFSWR HAFFQSDVLV QDVKYHSNPM ERVFSPAPGM
RVEIANPNTP AKTTIKVFEL SRASGKHEQT VEVSISGNRI SCNLIEYRTA SGKPASLPFL
FDYHSDRGYA PIHEVMSDRN DRIKEFYYRV WFGDNEKVPF DALLDEKFDG GRATVTSEAI
NDFVHAVGNN GEAFVDRPGK EVFAPMDFAI VVGWKAITKP IFPRKIDGDL LKLVHLSNGF
RMLPGASPLK KGDVLDTTAQ VNAVINQESG KMVEVCGTIT RNGEPIMEVV SQFLYRGDYT
DFENTFQRKS ETPMQLTLSS AKDIAILQSK EWFQIGDNEM DLLNQTLTFR LHSLVKFKNR
TVFSEVHTYG EVLLELPSKE IVQIASVDYQ AGDSHGNPVL DYLSRNGQPT DQPVHFENAI
PLHGKKPLAL KAPASNDTYA QVSGDFNPIH VSRVFAKHAG LPGTITHGMY TSAAVRSLVE
TWAAENHVGR VRSYHASLVG MVLPDDELDI KLSHTGMVSG RKIIKVEVSN KETEEKVLLG
EAEVEQPSTA YVFTGQGSQE QGMGMELYDT SKVAKEVWDR ADKHFMDNYG FSIVNIVKNN
PKELTIHFGG PRGKAIRQNY MAMTFETVGA DGQLKSEKIF KEVDEKTTSY TYRSPNGLLS
STQFTQPALT LMEKASFEDM RSKGLVQDDS SFAGHSLGEY SALASLAEVM PIESLVSVVF
YRGLTMQVAV ERDEQGRSNY AMCAVNPSRI SKTFNEQALQ YVVENIAAET TWLLEIVNLN
VANMQYVCAG DLRALDCLTN VLNFLKQQKI DIEHLMGTMS IEDVKEHLRS IIKECANQTK
AKAQPIELER GFATIPLRGI DVPFHSTFLR SGVKPFRNFL LKKINKTSID PAKLVGKYIP
NVTAKPFELT REYFEDVFRL TSSPRIGHIL QNWDKYETSD VLRNAASAA
//
