GRA7_GIBZE
ID GRA7_GIBZE Reviewed; 2060 AA.
AC I1S489; A0A098D0C5;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Fatty acid synthase subunit beta {ECO:0000303|PubMed:30395461};
DE EC=2.3.1.86 {ECO:0000305|PubMed:30395461};
DE AltName: Full=S-acyl fatty acid synthase thioesterase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=3.1.2.14 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=4.2.1.59 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=1.3.1.9 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] acetyltransferase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=2.3.1.38 {ECO:0000250|UniProtKB:Q8TGA1};
DE AltName: Full=Gramillins biosynthesis cluster protein FGSG_11656 {ECO:0000303|PubMed:30395461};
DE AltName: Full=[Acyl-carrier-protein] malonyltransferase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=2.3.1.39 {ECO:0000250|UniProtKB:Q8TGA1};
GN ORFNames=FG00037, FGRAMPH1_01T00131, FGSG_11656;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, AND PATHWAY.
RX PubMed=30395461; DOI=10.1021/jacs.8b10017;
RA Bahadoor A., Brauer E.K., Bosnich W., Schneiderman D., Johnston A.,
RA Aubin Y., Blackwell B., Melanson J.E., Harris L.J.;
RT "Gramillin A and B: cyclic lipopeptides identified as the nonribosomal
RT biosynthetic products of Fusarium graminearum.";
RL J. Am. Chem. Soc. 140:16783-16791(2018).
CC -!- FUNCTION: Fatty acid synthase subunit beta; part of the gene cluster
CC that mediates the biosynthesis of gramillins A and B, bicyclic
CC lipopeptides that induce cell death in maize leaves but not in wheat
CC leaves (PubMed:30395461). The nonribosomal peptide synthetase GRA1
CC incorporates respectively a glutamic adic (Glu), a leucine (Leu), a
CC serine (Ser), a hydroxyglutamine (HOGln), a 2-amino decanoic acid, and
CC 2 cysteins (CysB and CysA) (Probable). The biosynthesis of 2-amino
CC decanoic acid incorporated in gramillins could be initiated by a fatty
CC acid synthase composed of the alpha and beta subunits FGSG_00036 and
CC FGSG_11656 (Probable). The cytochrome P450 monooxygenase FGSG_15680
CC could hydroxylate the fatty acid chain (Probable). Subsequent oxidation
CC to the ketone by the oxidoreductase FGSG_00048 and transamination by
CC aminotransferase FGSG_00049 could form 2-amino-decanoic acid
CC (Probable). On the other hand, FGSG_15680 could also be responsible for
CC the HO-modified glutamine at the gamma-position (Probable). Whether
CC hydroxylation occurs on the fully assembled product or on the Gln
CC residue prior to assembly into the gramillins requires further proof
CC (Probable). The thioredoxin FGSG_00043 could also be required for the
CC disulfide-bond formation between CysA and CysB (Probable). The specific
CC involvement of the remaining proteins from the cluster is more
CC difficult to discern, but could have broader regulatory (FGSG_00040 and
CC FGSG_11657) or enzymatic functions (FGSG_00044 and FGSG_00045)
CC (Probable). The final C-domain of GRA1 does not possess the expected
CC sequence of a termination CT domain, often implicated in
CC macrocyclization and release of a cyclopeptidein fungal NRPs; and the
CC thioesterase FGSG_00047 may act in concert with the terminal C-domain
CC of GRA1 to catalyze the formation of the macrocyclic anhydride and
CC release of the products (Probable). {ECO:0000269|PubMed:30395461,
CC ECO:0000305|PubMed:30395461}.
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:30395461}.
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000250|UniProtKB:P19097}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; HG970332; CEF71865.1; -; Genomic_DNA.
DR RefSeq; XP_011315624.1; XM_011317322.1.
DR AlphaFoldDB; I1S489; -.
DR SMR; I1S489; -.
DR STRING; 5518.FGSG_11656P0; -.
DR GeneID; 23558475; -.
DR KEGG; fgr:FGSG_11656; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G00131; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR InParanoid; I1S489; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
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-EC.
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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.366.10; -; 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 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;
KW Hydrolase; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase;
KW Reference proteome; Transferase.
FT CHAIN 1..2060
FT /note="Fatty acid synthase subunit beta"
FT /id="PRO_0000450562"
FT DOMAIN 1549..1661
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..543
FT /note="Acetyltransferase (AT) domain"
FT /evidence="ECO:0000255"
FT REGION 600..845
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 1157..1640
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1679..2043
FT /note="Malonyl/palmitoyl transferase (MT/PT) domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 10..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 301
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000255|PIRSR:PIRSR005562-1"
FT ACT_SITE 1824
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2060 AA; 228604 MW; F24E6D1331407981 CRC64;
MFPGDMESKA SSMNGDQPSS PTPSSSTSVT IPTYTPTSMY DQELQFSRSV AKHVYEAAAT
LRAAFLCGFQ PYTDVASFAH DEIVSQLHYW SSFISFVNDP ANNQAFTRMD ILEVTRALVQ
CAEDTVLAGN DIHMIVAHLQ IPQSEKGRII KTFVTANSML GDQPEVEVSN LVRSSLDGES
TVYVIFGGQG NGDGYFAELA ELYEVYQPLV GDLVRSASDL FRHLTDKMDV NDCFSEGMEL
MAWIDKDNDT PIPSRPYLLS SAISFPLITL LQLLHFKISF HYSGCSFKDV QRFLAGVTGH
SQGIIAAAAI AAVDSPASFH ELSLQAMTVS FSMGVRIHQY YGPQVLPQLI TEACLAEGKP
IPTPMLSVRG LSIETLATTI QDLNKSLPRT KVQLEVGLRN NDSNYVITGD PMSLRGLCTH
FDHKKKALDI VYQFLPAAAP YHNSYLSIAA SRAIEDCQEI ILRGCDLKMP VFSTVDGSDL
RNNEGANLVP DLIRMVCCQV VNWPAALNMP GATHILDFGP GGAQGVGVLA NSMKAGQGVR
VIHATVLNGL NTELGYKPDL FDRSRKASER VSKPQPWVNS FQPTLTRFTE NKLVVSTRFT
RLFLQPPIMV AAMTPTTTSW DFVAAVMKAG FHAELACGGF HDRDSLSAAI TAIANQVEPG
TGITCNVIYS SPTSLRWQID ELEKLVAAGY QIDGLSIGAG VPSVEVVQGY VERLQLQHIA
LKPGSTEAIE RTLKIAKALQ PLPVVLQWTG GRGGGHHSNQ DFHAPLISMY GKIRAQDNVV
LVVGSGFGGP SDTLPYITGK WASDMGLPPM PVDGILLGSR VMVAKEAHTS TEAKHLIVAT
EGAPDDEWSG TYSRPTGGVL SVISEMRQPI HKIATRAVRL WHELDQTIFH LGPKERVAEI
TRRRDEIIRR LNHDYHRVWF GCSGPTRDPV ELDEMTYSEV LHRFVELAYV TAEHRWVHLS
WKKLFSELLT RTMSRLHRTS DSRSETLVDD LDDPYSTLAT LTDASAQLIT YEDSIYFLQL
FRRRGQKPVP FIPVLDADFE TWFKKDSLWQ SEDIAAVPNH DAQRVCILHG PVAAQYSTKV
DEPVGEILGN IHTAWVTAIL QTHYQGQSEL VPVFDNSPFH ASQVESSKTN TELSTPPLNH
GLWTLEQWIV HIVQSRDKNL NWAKALLASP RVLCGRRLVP NPFITTLSGL RSMDIHVAET
TKTGVGAGFT FFKIPLEETH QDLLDLTLQS NNEISIQISH YPTLQSAPIT LTHHMSCQFS
KLAMNKSLSD RSAMIRDFYR RIWLGTSHES SHKSIYDKFE CEPYTVTADA IRKYNDCTRL
PTSMPPTSWA TSEVPLDFAV VIAWKALVKP LFSRELEADI LKLLHVSNEI TLHSDHSPPM
VHDVLHTESQ VTEVVLQPSG KMVQVEAHVF RGKSCILDLK TRFLLVGNDT HRDHLFRRSI
LPPSEILLED EISAMQLVQS SWFQPLRDTS DLVGKRVVFQ LEDLMQFHEN GQIRCHQITG
CAMLDGSIVG NCYLETPDDA YLSLMGNILS QQTGSSSQPA IFETPLLLFE EQEISFTAPT
CEQTIAYSAA SGDSNPIHVS PVFASLAGLS SPIVHGMHIS AEVLQIVYTW LCASSMSRLK
KSHVLFAGKV CTGDRLAVSM KHTAMHRGLR VVEVQIHKNM AEELVFVGTY EIEQPLTALV
FTGQGSQKKG MGMDLRDKSA AARRIWDTAD DHFQHEYGFR ITDIVRHDPP SLTVHFGGVH
GRRVRSNYMA LTYERVASDG QIIEAKLFPT INENTTKYVF SSESGLLSST QFTQPALGLM
ELAIMADLEA RQLIPSNVTF AGHSLGEYSA LMAVGHIMPL EVFISTVFYR GLVMQSTVTY
DHHGRSKYAM CAVDPTRVST DFDGQKLGWL VTQIASEGQW LLEVVNHNVI DSQYVCAGEA
IALHCLGVVL DRIHYASKSF FDDGSFDLTD CIRESVKEIR KDRSKVVLSR SKASIPLKGL
DVPFHSSHLR SGVDPFRRRL QRSIKLDNAS PTKLIGRYIP NLTGKPFEVT RQYFNEVLRL
TGSIPIQQAL ESWDRVASTI
