ID TOXC_COCCA Reviewed; 2080 AA.
AC Q92215;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 24-JAN-2024, entry version 109.
DE RecName: Full=Fatty acid synthase beta subunit TOXC {ECO:0000303|PubMed:9057326};
DE EC=2.3.1.86 {ECO:0000250|UniProtKB:Q8TGA1};
DE AltName: Full=S-acyl fatty acid synthase thioesterase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=3.1.2.14 {ECO:0000250|UniProtKB:Q8TGA1};
DE AltName: Full=[Acyl-carrier-protein] malonyltransferase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=2.3.1.39 {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=TOX2 HC-toxin biosynthesis cluster protein TOXC {ECO:0000303|PubMed:9057326};
GN Name=TOXC {ECO:0000303|PubMed:9057326};
OS Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=5017;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=ATCC 90305 / SB111 / 2R15;
RX PubMed=9057326; DOI=10.1094/mpmi.1997.10.2.207;
RA Ahn J.-H., Walton J.D.;
RT "A fatty acid synthase gene in Cochliobolus carbonum required for
RT production of HC-toxin, cyclo(D-prolyl-L-alanyl-D-alanyl-L-2-amino-9, 10-
RT epoxi-8-oxodecanoyl).";
RL Mol. Plant Microbe Interact. 10:207-214(1997).
RN [2]
RP IDENTIFICATION WITHIN THE TOX2 CLUSTER, AND FUNCTION.
RX PubMed=8672886; DOI=10.1105/tpc.8.5.887;
RA Ahn J.H., Walton J.D.;
RT "Chromosomal organization of TOX2, a complex locus controlling host-
RT selective toxin biosynthesis in Cochliobolus carbonum.";
RL Plant Cell 8:887-897(1996).
RN [3]
RP TOX2 CLUSTER ORGANIZATION.
RX PubMed=11860263; DOI=10.1006/fgbi.2001.1305;
RA Ahn J.H., Cheng Y.Q., Walton J.D.;
RT "An extended physical map of the TOX2 locus of Cochliobolus carbonum
RT required for biosynthesis of HC-toxin.";
RL Fungal Genet. Biol. 35:31-38(2002).
CC -!- FUNCTION: Fatty acid synthase beta subunit, part of the diffuse TOX2
CC gene cluster that mediates the biosynthesis of the HC-toxin, cyclic
CC tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo
CC stands for 2-amino-9,10-epoxi-8-oxodecanoic acid (PubMed:9057326,
CC PubMed:8672886). HC-toxin is a determinant of specificity and virulence
CC in the interaction between the producing fungus and its host, maize
CC (PubMed:9057326). TOXC contribute to the synthesis of the decanoic
CC backbone of 2-amino-9,10-epoxi-8-oxodecanoic acid, an essential
CC precursor for the production of the major forms of HC-toxin by the non-
CC ribosomal peptide synthetase HTS1 (PubMed:9057326).
CC {ECO:0000269|PubMed:8672886, ECO:0000269|PubMed:9057326}.
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; HC-toxin biosynthesis.
CC {ECO:0000269|PubMed:9057326}.
CC -!- DISRUPTION PHENOTYPE: Does not affect growth and sporulation, but
CC impairs the production of HC-toxin and related pathogenicity.
CC {ECO:0000269|PubMed:9057326}.
CC -!- MISCELLANEOUS: The genes involved in HC-toxin biosynthesis, called
CC collectively TOX2, are organized into a diffuse cluster that spans >500
CC kb. All of the known genes are duplicated or triplicated within this
CC region, with some variation in copy number and chromosomal location
CC among different race 1 strains. {ECO:0000269|PubMed:11860263,
CC ECO:0000269|PubMed:8672886}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U73650; AAC62818.1; -; Genomic_DNA.
DR AlphaFoldDB; Q92215; -.
DR SMR; Q92215; -.
DR UniPathway; UPA00874; -.
DR PHI-base; PHI:97; -.
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: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-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:RHEA.
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; 6.10.60.10; -; 1.
DR Gene3D; 6.20.240.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
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; Fatty acid metabolism; Hydrolase;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Multifunctional enzyme; NAD;
KW NADP; Oxidoreductase; Transferase.
FT CHAIN 1..2080
FT /note="Fatty acid synthase beta subunit TOXC"
FT /id="PRO_0000180291"
FT DOMAIN 170..397
FT /note="Starter acyltransferase (SAT)"
FT /evidence="ECO:0000255"
FT DOMAIN 1544..1662
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
FT DOMAIN 1682..2046
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000255"
FT REGION 585..830
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 1155..1644
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1683..2046
FT /note="Malonyl/palmitoyl transferase (MT/PT) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 276
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000255|PIRSR:PIRSR005562-1"
FT ACT_SITE 1828
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2080 AA; 232268 MW; 424D3C489EF67087 CRC64;
MLLTAQIPES LTPFSISHGS LSVSWLLPYR LHCYATRLYR TFEATLAARS DNSEHPITLL
SSVELAAHYM CYVAHETQAN TDRACTQTHD ISKLLLEDFE ATFLRSNDIH TLASALPSSD
SAKDELLRCY YETCFITKHN TPLNESALLK AAREGIVSLY TTFSGQGCGG RYFDELRELF
RLYPSFVGTL ISESGNLFRE LASNPSAGRL FSKGFDIMAW LHHPQTTPDT EYLISAPVSF
PIIGLVQLGH YAVSCRAMGL DPGAFQRSIR GSTGHSQGIV VAAAMSAADS WEAFDRLAIS
CLTVLFWIGV RSQQAAPQMS LSPAQIQDSI DHNEDVPSPM LSIIGLSRLD VQMHIDSINH
YLPQSEHISI SLVNGGRHIV VSGLPSTLYR FNLLLRKIKV PDHSGQPRAT SKQKKAQFSA
RFLPITVPFH SHHLVSVGSV LEEDLKNVFI GSKDLGFPVF NTYTGRDLRA EVIGNIVPAL
VRMVTQYPVF WGAAVEFPGA THILEFGPGG LSGSGALTSH IKNGTGVRVI FAGLTSGSNR
QVGYKQELFA RDTCHVKFAD DWSRKYAPSL VRTSNNSIVV NTKMSRLLGL PPIMVGGMTP
TTAAWGFVAA TMNAGYHIEL AAGGYSDANA FENALLNIQK TTASGRGITV NLIYLSSHAV
NWQIPLLRRL IIDGFRIEGI TIGGGVPSID VAKEYITTLG IKHIGFKPGP TTAIDAVIEI
AQANPTFPVF LQWTGGRSGG HHSNEDFHQP ILETYDRIRQ CDNIILIAGS GFGGAADTYP
YITGEWSLRY DFPPMPFDGC LLGSRVMVAK EARTSPAAKR VIVETEGLND NEWRRTYEEA
AGGIITVQSE MGQPIHKIAT RGVLFWAKLD QMIFSLPKEK RIAELQKHRS WIIKGLNDDF
QKPWFGRDSA DQVVELRDMT YAEVLRRMVQ LLYVKHQRRW IHSSYAVLFK AFVNRLEERF
TTKTVQSYLI QDCKTIDDPY NIITVVLLQY QQAIKETILT PDVEYFLLLC KRRGQKPVPF
VPALDEDFEF FFKKDSLWQS EDLEAVVDQD VGRTCILQGP VAAKYSVKVD EPIAEILGSI
HQGHVTRLRE ERYCATLDSI PFVEYFGGES IQLDMSSLAD GIEQSHNEQA SIYSLPSSLS
MPLPAVDVWM SLLAGKSRSW RHAIMSAGIV IQENKCVANP MRRLFAPAHG IRVQIRKPDV
PSQTEVVLEE QQESGIYEVA VRAGLNEDGE IIVEMFERRN MSDLVVSLPC DSGTKPEYGY
APIREIMEDR NERIRRFYWS IWFGKSHPIL EGSLSDSFEC GKEKITRQHV ESFIQAINNS
TRTHKNFLEP ATNVSISFAI PVAWKAIVKP LFLNALNGDL LQLVHLSNEF RMTPGAEPLK
IGEEVSTVAR INAIMNQDSG KMVEVSAAVL RGKEIVVEII SRFLYRGAFV DFKDTFQWRD
EPLMQIQLAT SKHIAVLRTR EWFVPTQGCN IDLVGHTLTF QMRSLYKFQS KTVFRRIETH
GKVTLELAPQ KIVQVATVQY EVGICHSNTV IEFLDRYGSY SQNSVDFEDP VSVPNNGESL
VICAPSSNEA YARTSGDLNP IHVSRTFAEY AGLPGLITHG MYCSAAIQDL VERLVADGNA
GRIRQFSMSF VGMVLPNQKL EVKLEHIGMV EGMIRLHIEA RAQETGHRVI VGEAKITQKM
TTYVFTGQGS QEKGMGMDLY NQCPAAREVW DRGDKYFLHK YGFAITTIVR DNPKQLTVHF
GGRQGEAIRQ NYINMKVETV AEDGSIQYEK LFKDVDHNTQ FYTFRSPTGL LSATQFTQPA
LSLMARASFE HLQIQGLVDG NCYYAGHSLG EFSALAAVAG IMSVESQALI AFYRGLTMQK
AVNRDESGRS NYSMCAVDPS RISATYDEEA FLTIVREIAA ETGWLLEVVN FNVANKQYVC
AGNLHALDTL AGVTDRLRLL QINASEMEEC LHEIIRQCVQ ETKSKSTPLE LTRGIATIPL
QGIDVPFHST FLRGGVRHFR EFLHENIDKR NINPAKLIGR YIPNVTARSF QISKDYFQYV
YDLTGSSQLR DALKNWDIYE KSNGEESNGV EECSECRNSL
//
