EFUC_HORCR
ID EFUC_HORCR Reviewed; 551 AA.
AC A0A2Z4HPY5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Acetyltransferase efuC {ECO:0000303|PubMed:30051576};
DE EC=2.3.1.- {ECO:0000305|PubMed:30051576};
DE AltName: Full=Enfumafungin biosynthesis cluster protein C {ECO:0000303|PubMed:30051576};
GN Name=efuC {ECO:0000303|PubMed:30051576};
OS Hormonema carpetanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Dothioraceae; Hormonema.
OX NCBI_TaxID=284138;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX PubMed=30051576; DOI=10.1111/1462-2920.14333;
RA Kuhnert E., Li Y., Lan N., Yue Q., Chen L., Cox R.J., An Z., Yokoyama K.,
RA Bills G.F.;
RT "Enfumafungin synthase represents a novel lineage of fungal triterpene
RT cyclases.";
RL Environ. Microbiol. 20:3325-3342(2018).
CC -!- FUNCTION: Acetyltransferase; part of the gene cluster that mediates the
CC biosynthesis of enfumafungin, a glycosylated fernene-type triterpenoid
CC with potent antifungal activity, mediated by its interaction with beta-
CC 1,3-glucan synthase and the fungal cell wall (PubMed:30051576). The
CC pathway begins with the terpene cyclase-glycosyl transferase fusion
CC protein that most likely uses 2,3-oxidosqualene as substrate and
CC catalyzes glycosylation immediately after cyclization (Probable). The
CC fernene glycoside then could be processed by the desaturase efuI which
CC catalyzes isomerization of a double bond established by efuA to form
CC the core structure (Probable). The latter would then undergo a series
CC of hydroxylations in unknown order at C-2, C-19, C-23 and C-25, which
CC would be catalyzed by two of the three cytochrome P450 monooxygenases
CC efuB, efuG or efuH (Probable). The hydroxy-group at C-25 becomes
CC oxidized by the dehydrogenase efuE to enable a spontaneous, non-
CC enzymatic hemiacetal formation with C-23 (Probable). After
CC hydroxylation at C-2, acetylation by the acetyltransferase efuC takes
CC place (Probable). The final steps in enfumafungin biosynthesis require
CC expansion of the 5-membered ring by lactonization via a Baeyer-Villiger
CC reaction mediated by one of the BGC's cytochrome P450 monooxygenases
CC (efuB, efuG or efuH) followed by ring cleavage (Probable). This type of
CC reaction would establish a double bond between C-20 and C-21 which
CC could be reduced by the reductase efuL to form the final product
CC (Probable). {ECO:0000269|PubMed:30051576, ECO:0000305|PubMed:30051576}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:30051576}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000305}.
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DR EMBL; MF611884; AWW17212.1; -; Genomic_DNA.
DR UniPathway; UPA00213; -.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00296; MetX_acyltransf; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR008220; HAT_MetX-like.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Transferase.
FT CHAIN 1..551
FT /note="Acetyltransferase efuC"
FT /id="PRO_0000454460"
FT DOMAIN 141..406
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..151
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:Q5AT15"
FT REGION 434..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 253
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT ACT_SITE 495
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT ACT_SITE 532
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT BINDING 533
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT SITE 290
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000250|UniProtKB:Q5AT15"
SQ SEQUENCE 551 AA; 60251 MW; B2BA7765BA152C8F CRC64;
MSAPRTALSS ARQLSNGLIR RTNPRKRFLP LPSTVRSFTN NKPLRSQATA AQEPIVESER
PSPVTSVNQP LSFPCLDALD TKTQSLTKQK KSLSGPEPSY AAGETEHFHS ASPILLDWGG
VLPEFDIAYE TWGTLNADKS NAILLHTGLS ASSHAKSTAK NPKPGWWEKF IGPGAPLDTD
KYHIICTNVL GGCYGSTGPS SIDPLAENNT SSAQKDRYAT RFPILTMQDM VRAQFRLLDW
MGIDALYASV GSSMGGMQSL AACVLEPSRV GKVVSVSGCA RSHPYSIAMR HTQRQVLMND
PAWSSTRGNY YPSIPPHAGM KLAREIATVT YRSGPEWEQR FGRRRADPSK PPALCPDFLI
ETYLDHAGEK WCLEYDANSL LYVSKAMDLF DLGDEHMRTL DGVRKSNAWK LDGFAAGTAK
EEEKAGLCNL TLPDTPYEEQ DETSSELLAS SPEEAKRARE TSSAALIAEE PPEDLVKGLQ
ALSGTPALVM GVASDILFPA WQQREIAAAL RKAGNRRVTH VELGEDRSLF GHDTFLLDLE
GVGGEIRRFL G
