ATNB_ARTSZ
ID ATNB_ARTSZ Reviewed; 266 AA.
AC A0A455LLX2;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Short-chain dehydrogenase/reductase atnB {ECO:0000303|PubMed:29797385};
DE EC=1.1.1.- {ECO:0000305|PubMed:29797385};
DE AltName: Full=Arthripenoid biosynthesis cluster protein B {ECO:0000303|PubMed:29797385};
GN Name=atnB {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], DISRUPTION PHENOTYPE, 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: Short-chain dehydrogenase/reductase; part of the gene cluster
CC that mediates the biosynthesis of the meroterpenoids arthripenoids
CC (PubMed:29797385). The pathway begins with the HR-PKS atnH that
CC catalyzes two chain-extension steps to form a reduced triketide, which
CC then primes the SAT domain in the NR-PKS atnG to initiate three more
CC cycles of extension to give a linear hexaketide corresponding to the
CC polyketide part of arthripenoids (PubMed:29797385). The FAD-dependent
CC monooxygenase atnJ then performs an oxidative decarboxylation at C11 of
CC the atnH/atnG product, via an electrophilic aromatic hydroxylation with
CC concomitant ipso-decarboxylation (PubMed:29797385). The membrane-bound
CC polyprenyl transferase atnF then introduces a farnesyl group before the
CC FAD-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 -!- DISRUPTION PHENOTYPE: Abolishes the production of arthripenoids but
CC leads to the accumulation of a new compound that has a keto group at
CC position C4. {ECO:0000269|PubMed:29797385}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; MH183008; AYO60875.1; -; mRNA.
DR AlphaFoldDB; A0A455LLX2; -.
DR SMR; A0A455LLX2; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NAD; NADP; Oxidoreductase.
FT CHAIN 1..266
FT /note="Short-chain dehydrogenase/reductase atnB"
FT /id="PRO_0000452561"
FT ACT_SITE 166
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 10..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 32..33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 34..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 124
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 131..133
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
SQ SEQUENCE 266 AA; 28695 MW; ADDF22526E24B417 CRC64;
MSSWAITGAS RGIGFEFAKQ LSADGSNQVF ALIRSEPSAE LAELSSGREN LHVIQADVTD
AQGLSEAAAK VGELTGNKLD VFISNACHPG LDLRFHPTSA FLGKEKELKE EIDACMNVNL
LGAINSINCF LPLIRNGELK KIIYITSPSG DAEFTRKCGV TVTVGYSITK AAMNLVMSKY
AAELKGEGIK TLSLSPGWVD TDGTRDMAPT PEILEMALQV FQKFKPDLTG LMSVEESVRM
QLNVINGLTV KQSGLALSHH GDYNWL