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   25-MAY-2022, entry version 81.
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   EnsemblFungi; BAE56608; BAE56608; AO090001000045.
DR   GeneID; 5990581; -.
DR   KEGG; aor:AO090001000045; -.
DR   VEuPathDB; FungiDB:AO090001000045; -.
DR   HOGENOM; CLU_023194_25_2_1; -.
DR   OMA; ADPSHCT; -.
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   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   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 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