ID ACLE_ASPOR Reviewed; 366 AA.
AC Q2UPA7;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Dehydrogenase aclE {ECO:0000303|PubMed:25302411};
DE EC=1.-.-.- {ECO:0000305|PubMed:25302411};
DE AltName: Full=Aspirochlorine biosynthesis protein E {ECO:0000303|PubMed:25302411};
DE Flags: Precursor;
GN Name=aclE {ECO:0000303|PubMed:25302411}; ORFNames=AO090001000045;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=25302411; DOI=10.1002/anie.201407624;
RA Chankhamjon P., Boettger-Schmidt D., Scherlach K., Urbansky B., Lackner G.,
RA Kalb D., Dahse H.M., Hoffmeister D., Hertweck C.;
RT "Biosynthesis of the halogenated mycotoxin aspirochlorine in koji mold
RT involves a cryptic amino acid conversion.";
RL Angew. Chem. Int. Ed. 53:13409-13413(2014).
CC -!- FUNCTION: Dehydrogenase; part of the gene cluster that mediates the
CC biosynthesis of aspirochlorine (or antibiotic A30641), an unusual
CC halogenated spiro compound with distinctive antifungal properties due
CC to selective inhibition of protein biosynthesis, and which is also
CC active against bacteria, viruses, and murine tumor cells
CC (PubMed:25302411). The non-ribosomal peptide synthetase (NRPS) aclP is
CC responsible the formation of the diketopiperazine (DKP) core from the
CC condensation of 2 phenylalanine residues (PubMed:25302411). One Phe
CC residue is tailored into chlorotyrosine by hydroxylation and
CC chlorination, whereas the second Phe undergoes an unprecedented C-C
CC bond cleavage to be converted into glycine (PubMed:25302411). After
CC formation of the DKP, sulfur is incorporated into the DKP by
CC conjugation with glutathione by aclG, followed by its stepwise
CC degradation to the thiol by aclI, aclJ and aclK, and the dithiol
CC oxidation by aclT (PubMed:25302411). In addition, oxygenases (aclB,
CC aclC, aclL and aclO) and O-methyltransferases (aclM and aclU) act as
CC tailoring enzymes to produce the intermediate dechloroaspirochlorine
CC (PubMed:25302411). Ultimately, chlorination of dechloroaspirochlorine
CC by the halogenase aclH is the last step in the aspirochlorine pathway
CC (PubMed:25302411). {ECO:0000269|PubMed:25302411}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25302411}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AP007154; BAE56608.1; -; Genomic_DNA.
DR RefSeq; XP_001818610.1; XM_001818558.2.
DR AlphaFoldDB; Q2UPA7; -.
DR SMR; Q2UPA7; -.
DR STRING; 510516.Q2UPA7; -.
DR GlyCosmos; Q2UPA7; 1 site, No reported glycans.
DR EnsemblFungi; BAE56608; BAE56608; AO090001000045.
DR GeneID; 5990581; -.
DR KEGG; aor:AO090001000045; -.
DR VEuPathDB; FungiDB:AO090001000045; -.
DR HOGENOM; CLU_023194_25_2_1; -.
DR OMA; CWEEISL; -.
DR OrthoDB; 2735190at2759; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43708; CONSERVED EXPRESSED OXIDOREDUCTASE (EUROFUNG); 1.
DR PANTHER; PTHR43708:SF1; GALACTOSE_LACTOSE METABOLISM REGULATORY PROTEIN GAL80; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..366
FT /note="Dehydrogenase aclE"
FT /id="PRO_0000441203"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 366 AA; 40231 MW; D2C71A465FA0365D CRC64;
MSKRIRLGIV GLSADPSHCT NYIHKIPLTT TPLKEKYEIT AVSMSSPEKA EAAAIAHGLP
RERGYHSVES LAKDPDVDLV VVSVKVPRRA ELAMAAIEAG KDVYVEWPFA SNLAAAEALA
QRARERQVKS MVGLPTRLAP QVLKMKEILR SGSLGRILAT NLLVTDDLFL KFHADKRHSH
DKTNGANIVT IAGGHLLDAM AFLLGEFTTL HAHTSMLFPK PVLCDTDGNL KTGQFNDSPD
TFTMHGKIGI SEVPVSVCMY SHPPTTPNLF QWVITGEKGS LKMEGPSLMI HAIPPKLMMT
SFGSETVCWE EISLENTIVS GAEYQAWLDN DTERIVTLDE AVVRYRMVDA ILRSAESGQC
TSYRYD
//
