ATNC_ARTSZ
ID ATNC_ARTSZ Reviewed; 435 AA.
AC A0A455LM26;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Acetyltransferase atnC {ECO:0000303|PubMed:29797385};
DE EC=2.3.1.- {ECO:0000305|PubMed:29797385};
DE AltName: Full=Arthripenoid biosynthesis cluster protein C {ECO:0000303|PubMed:29797385};
GN Name=atnC {ECO:0000303|PubMed:29797385};
OS Arthrinium sp.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Apiosporaceae; Arthrinium;
OC unclassified Arthrinium.
OX NCBI_TaxID=1756131;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND PATHWAY.
RC STRAIN=NF2194;
RX PubMed=29797385; DOI=10.1002/anie.201804317;
RA Zhang X., Wang T.T., Xu Q.L., Xiong Y., Zhang L., Han H., Xu K., Guo W.J.,
RA Xu Q., Tan R.X., Ge H.M.;
RT "Genome mining and comparative biosynthesis of meroterpenoids from two
RT phylogenetically distinct fungi.";
RL Angew. Chem. Int. Ed. 57:8184-8188(2018).
CC -!- FUNCTION: Acetyltransferase; part of the gene cluster that mediates the
CC biosynthesis of the meroterpenoids arthripenoids (PubMed:29797385). The
CC pathway begins with the HR-PKS atnH that catalyzes two chain-extension
CC steps to form a reduced triketide, which then primes the SAT domain in
CC the NR-PKS atnG to initiate three more cycles of extension to give a
CC linear hexaketide corresponding to the polyketide part of arthripenoids
CC (PubMed:29797385). The FAD-dependent monooxygenase atnJ then performs
CC an oxidative decarboxylation at C11 of the atnH/atnG product, via an
CC electrophilic aromatic hydroxylation with concomitant ipso-
CC decarboxylation (PubMed:29797385). The membrane-bound polyprenyl
CC transferase atnF then introduces a farnesyl group before the FAD-
CC dependent monooxygenase atnK functions as the first epoxidase on
CC terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8'
CC catalyzed by atnA (PubMed:29797385). The terpene cyclase/mutase atnI
CC then initiates the sequential tricyclic ring formation through
CC protonation of the terminal epoxide and catalyzes the regioselective
CC and stereoselective 6/6/6-tricyclic ring formation (PubMed:29797385).
CC The cytochrome P450 monooxygenase atnM is responsible for hydroxylating
CC both C1' and C10' (Probable). The next steps may involve ketoreduction
CC and acetyl transfer by the ketoreductase atnB and the acetyltransferase
CC atnC, and lead to the production of arthripenoid B, the final
CC biosynthetic product of the atn cluster (PubMed:29797385). The
CC hydroquinone moiety in arthripenoid B is prone to undergo spontaneous
CC oxidation to afford a benzoquinone compound, a key intermediate for
CC generating structure diversity (Probable). For instance, addition of a
CC cysteine followed by ring contraction gives arthripenoid A,
CC tautomerization gives the main product arthripenoid C, addition of a
CC molecular of water or amine affords arthripenoid D or E, respectively,
CC and loss of one water forms arthripenoid F (Probable).
CC {ECO:0000269|PubMed:29797385, ECO:0000305|PubMed:29797385}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:29797385}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the wax synthase family. {ECO:0000305}.
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DR EMBL; MH183009; AYO60876.1; -; mRNA.
DR AlphaFoldDB; A0A455LM26; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR044851; Wax_synthase.
DR InterPro; IPR032805; Wax_synthase_dom.
DR PANTHER; PTHR31595; PTHR31595; 1.
DR Pfam; PF13813; MBOAT_2; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..435
FT /note="Acetyltransferase atnC"
FT /id="PRO_0000452562"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 435 AA; 49163 MW; E30AA1E5DC81E9AB CRC64;
MALVNNPIQA FANVALLFAV QILIPAFLII TTPKYSWLRY FGIPCIAFPA YLIFQLAPTL
SNSIFHNSFL ACEGILVVAH CVNLLLILQD GGLTWSDLRR SGVAGEKSET PPDATFLRKL
ISAVRLVVSL RGVDTPWEAK NTPPHPSSLG PGGGSRASFL IRQGAILAWQ YLFLDVLLEV
TKQEPPENTD KFYRPGMEYE YLNLTAEERF IRAFMPFVSW FVVSRLLLDS TWRALSILFV
ASGLGSPQSW RPLFGSMWDA YTLRNFWGKF WHQILRWPFT SNVNFLTRRV VKLPVPSLLD
RYTNNFLVFL LSGILHAVSA NIMGLSAVES GSIPYFSSFA LGMMLEDGVQ AFYNRLHADK
ERKTGIWKKV VGFIWVVFWM SLTSPWYMFP SRRKVAGEAA WVLPFNLTEV IGMPMMWGLL
GTFGMLVKWA FGTSL
