TOXC_COCCA
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 25-MAY-2022, entry version 103.
DE RecName: Full=Putative fatty acid synthase subunit TOXC;
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase;
DE EC=4.2.1.59;
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH];
DE EC=1.3.1.9;
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] acetyltransferase;
DE EC=2.3.1.38;
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] malonyltransferase;
DE EC=2.3.1.39;
DE Includes:
DE RecName: Full=S-acyl fatty acid synthase thioesterase;
DE EC=3.1.2.14;
GN Name=TOXC;
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 {ECO:0000312|EMBL:AAC62818.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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).
CC -!- FUNCTION: Essential role in the production of HC-toxin and in
CC pathogenicity of the fungus on maize. May contribute to the synthesis
CC of the decanoic backbone of 2-amino-9,10-epoxi-8-oxodecanoic acid. This
CC protein contains domains similar to those of a fatty acid synthase beta
CC subunit, namely: [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:0000269|PubMed:9057326}.
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 -!- 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 -!- 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 -!- 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 -!- 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 -!- PATHWAY: Mycotoxin biosynthesis; HC-toxin biosynthesis.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000305}.
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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: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: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:UniProtKB-KW.
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 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="Putative fatty acid synthase subunit TOXC"
FT /id="PRO_0000180291"
FT DOMAIN 1538..1667
FT /note="MaoC-like"
FT REGION 1..468
FT /note="Acetyltransferase"
FT /evidence="ECO:0000250"
FT REGION 481..869
FT /note="Enoyl reductase"
FT /evidence="ECO:0000250"
FT REGION 1155..1644
FT /note="Dehydratase"
FT /evidence="ECO:0000250"
FT REGION 1645..1865
FT /note="Malonyl/palmitoyl transferase"
FT /evidence="ECO:0000250"
FT ACT_SITE 276
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 1828
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000250"
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
