ID A0A3N2Q288_9PEZI Unreviewed; 2104 AA.
AC A0A3N2Q288;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Fatty acid synthase subunit beta dehydratase {ECO:0000313|EMBL:ROT40735.1};
GN ORFNames=SODALDRAFT_103778 {ECO:0000313|EMBL:ROT40735.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT40735.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT40735.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT40735.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
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 -!- 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 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 -!- 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 -!- 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 -!- 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 -!- 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; ML119052; ROT40735.1; -; Genomic_DNA.
DR STRING; 1314773.A0A3N2Q288; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000272025; 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:0016297; F:acyl-[acyl-carrier-protein] hydrolase 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 6.10.60.10; -; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005562};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
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:UP000272025};
KW Transferase {ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1696..2015
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1949..1976
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 286
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1840
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2104 AA; 232382 MW; A76AA2C2854233F0 CRC64;
MYGTGTGPQT GVSTPRSNSS LRPLTLRHGS LETSFLAPTS LHFHAQQLND RFAATLPTAT
DELAQDDEPS SVAELLARYM GFVANEIEKG EDDEQGSYEA VLKIVLVEFE RAYLQGNEVH
ALVATLPGID AKKLEVVRSY YHARITVGRP IKEHESALFR AAEDGAAGIY SIFGGQGNIE
EYFDELREIY KTYWPLLGGL IHDAAELLQT LSKHPGAEKL YPKGLDILNW LEHEDATPDV
DYLVSAPVSF PLIGLVQLAH YEVTCKVMGI DPGKMRDRLK GSTGHSQGVV LAAATAAASS
WESWADIAKS TLTILFWIGA RSQQVFPRTS LAPTMMRESI DNGEGAPTPM LSIRDLSQAE
VQKHVDATNQ YLPADRHISI SLINSPRNLV VTGPPISLCG LNAQLRKVKA ATGLDQNRIP
HTERKSRFVN RFLPISAPFH SKYLAEATEL IDADLKDVQI DSESLAIPVF DTNSGKDIRE
EVNGNIVPNL VRLITRDPVN WEKATIFPGA THVLDFGPGG ISGLGILASR NKEGTGVHVI
LAGSVNGTIT EVGYKSELFD RDEEHAVRYA MDWVKEFGPR LIRTVSGQTF VDTKMSRLLG
LPPVMVAGMT PTTVPWDFVA ATMNAGYHVE LAGGGYYNGK TMTEALSKIE NAIPAGRGIT
VNLIYVNPRA MGWQIPLIGR LRAEGVPIEG LTIGAGVPSI EVAQEYIETL GLKHIAFKPG
SVDAIQSVIN IAKANPDFPV ILQWTGGRGG GHHSYEDFHQ PILTMYGRIR RTPNIVLVAG
SGFGGAEDTY PYLTGEWSRR FGYPPMPFDG TLFGSRMMVA KEAHTSKAAK QAIVDAPGVG
DEGWEQTYKG PAGGVVTVRS EMGEPIHKLA TRGVLFWAEM DKKIFSLPKE KRVAELKKNR
SYIIKKLNDD FHKVWFGRNR AGEAVDLEDM TYGEVVRRMV DLLYVRHESR WIDPSFKKLT
GDFIHRVEER FTSGRDHASL LQDFGELDTP FQTVTRILAS YPEAEEQIIN AQDVQHFLML
CQRRGQKPVT FVPALDENFE FFFKKDSLWQ AEDLGAVIDQ DVGRTCILQG PMAAKYSTKM
DEPIQDILDS IHNAHIAGLT QDLYDGDANA IPVIEYFGGK LGEPEIPVED VDGLVTSYDE
TKNTYRLVAL PGTTMPSEEA WLALLAGPRR SWRHALLTSD VLVQGQKFQT NPMKRIFAPV
RGLFVEIHYP NDPSRTRIVV KEQPRHGKYV DVLEVKLVGK NEIVVSMIKD TTALGAPVSL
PLKFTYHPET GYAPIHEVME SRNDRIKAFY WRTWFGHDAL DLDADVTSKF DGGSAVITGE
GINDFVHAVG NTGEAFVERP GKTVYAPMDF AIVVGWKAIT KPIFPRTIDG DLLKLVHLSN
QFRMMPGAEP LQKGDEVNTT AQVNAVINQD SGKMVEVCGT IWRRGEAVME VTSQFLYRGT
YTDYENTFQR NTETPVQVHL ATTKDVSILK SKEWFNIDDL PQDIQLLGKT LTFRLQSFLK
FKNKTVFSSV QTFGQVLLEL PTKEVIQVAS VDYRAGVSHG NPVIDYVERN GTPLDQPLNF
ENPIPLSGKT PLQLRAPSSN ETYARVSGDY NPIHVSRIFA AYANLPGTIT HGMYSSAAVR
SLVETWAAEN NIGRVRSFHA SLAGMVLPND EILVKLEHVG MVAGRKIIKV EATNKDTGDK
VLLGEAEIEQ PVTAYVFTGQ GSQEQGMGME LYASSPVAKE VWERADKYLL DNYGFSITNI
VRNNPKELTI HFGGPRGKAI RQNYMAMTFE TVAADGSIKS EKIFKEIDEK TTSYTYRSPT
GLLSATQFTQ PALTLMEKAS FEDMKSKGLV PRDCTFAGHS LGEYSALAAL AEVMPIESLV
SVVFYRGLTM QVAVERDAAG RSNYSMCAIN PSRISKTFNE EALQFVVNNI AEETGWLLEI
VNYNIANMQY VAAGDLRALD TLTGVTNLLK VQKIDVDEMR ANIEEAKGAL REIIRGCAED
TLRKPTPLEL QRGFATIPLK GIDVPFHSTF LRSGVKPFRS FLLKKINRTT IDPSKLVGKY
IPNVTAKPFA LTREYFEEVY KLTNSPKIAS VLANWDSYTQ DAPAGGVDGV NGVNGHHEGP
GSAA
//
