ACLI_ASPOR
ID ACLI_ASPOR Reviewed; 420 AA.
AC Q2UPB9;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Probable aminotransferase aclI {ECO:0000303|PubMed:25302411};
DE EC=2.6.1.- {ECO:0000305|PubMed:25302411};
DE AltName: Full=Aspirochlorine biosynthesis protein I {ECO:0000303|PubMed:25302411};
GN Name=aclI {ECO:0000303|PubMed:25302411}; ORFNames=AO090001000033;
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: Probable aminotransferase; part of the gene cluster that
CC mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an
CC unusual halogenated spiro compound with distinctive antifungal
CC properties due to selective inhibition of protein biosynthesis, and
CC which is also 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=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P00509};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25302411}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255}.
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DR EMBL; AP007154; BAE56596.1; -; Genomic_DNA.
DR RefSeq; XP_001818598.1; XM_001818546.1.
DR AlphaFoldDB; Q2UPB9; -.
DR SMR; Q2UPB9; -.
DR EnsemblFungi; BAE56596; BAE56596; AO090001000033.
DR GeneID; 5990569; -.
DR KEGG; aor:AO090001000033; -.
DR VEuPathDB; FungiDB:AO090001000033; -.
DR HOGENOM; CLU_017584_1_2_1; -.
DR OMA; CSITQAN; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..420
FT /note="Probable aminotransferase aclI"
FT /id="PRO_0000441202"
FT MOD_RES 264
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P00509"
SQ SEQUENCE 420 AA; 46046 MW; 3F99C29408719C4A CRC64;
MASAGAGLSK RGASNVDAIM PGIRAALLER TRPTVPRIDL STAENWLLRN EVIELTKDAI
RDGLKPHHLS YPNEFAGDAD LIKALAAFVN EYFHPHIPVE PDHIATAPGA ATCLNTFLYN
LCEPGEGILV PAPFWNGFDW LFTARSSAVP VMVHVERSAD TLTAKLIPAL EKAYEESKIP
IRGLLLTNPQ NPYGQCYPRS VMEDCIRFCH SKGIHYISDE VYALSNFENP ELPDAPPFVS
ALQIDVKGIG CDLSRVHTFW STSKDFGSSG FRVGCSITQA NEAMHVALAL ASNTESSSLS
AVASTALLTS PRLPELLQLN AQRLQEAYCL MTNFLKKHQI EYIPANSAPF LFARVAPQAQ
TWEDEKAVIA QLKEAGVNVS GGKAYHVNED QKGWARLTFA LETSRAEEAI KRMETVLGKQ
