ACLT_ASPOR
ID ACLT_ASPOR Reviewed; 334 AA.
AC Q2UPB4;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Thioredoxin reductase aclT {ECO:0000303|PubMed:25302411};
DE EC=1.8.1.- {ECO:0000305|PubMed:25302411};
DE AltName: Full=Aspirochlorine biosynthesis protein T {ECO:0000303|PubMed:25302411};
GN Name=aclT {ECO:0000303|PubMed:25302411}; ORFNames=AO090001000038;
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: Thioredoxin reductase; part of the gene cluster that mediates
CC the 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:E9RAH5};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:E9RAH5};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25302411}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:E9RAH5}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AP007154; BAE56601.1; -; Genomic_DNA.
DR RefSeq; XP_001818603.1; XM_001818551.1.
DR AlphaFoldDB; Q2UPB4; -.
DR SMR; Q2UPB4; -.
DR EnsemblFungi; BAE56601; BAE56601; AO090001000038.
DR GeneID; 5990574; -.
DR KEGG; aor:AO090001000038; -.
DR VEuPathDB; FungiDB:AO090001000038; -.
DR HOGENOM; CLU_031864_5_0_1; -.
DR OMA; MALHTVW; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="Thioredoxin reductase aclT"
FT /id="PRO_0000441210"
FT BINDING 16..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT BINDING 38..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT BINDING 93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT BINDING 122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT BINDING 294
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT BINDING 302..303
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
SQ SEQUENCE 334 AA; 36255 MW; 81BDE004EE5A8CF0 CRC64;
MCDSSQSTAD VLIIGGGPAG SNAAWELGQA HHRVILFNAS IDRLRDPDVN TASTRPALDL
LLHSRRKTPD VFRPFRQEIG KESSEVSVHN QRITQVQRLP NGFFQAEDDV GHVWTAKVLV
LADGAEEILP DIDGYDTCWE QQRILTHPAE DEPRSLISSC LAVLAVGDLA ELTMALHTVW
QARQFAASVR VYTHGDEDLA RALETRISPD ARIAIQTTPI QSLQPGSDSP SQVVVHLADG
SSIVESHVYH RPASQLQGPF ARQLNLELTE SGAIRISARV PYMTSLDGVY AGGDCASLGQ
RTLFKALAMG QGLAAAVAAR LERGNWGNAV EEQD
