ID   ACLK_ASPOR              Reviewed;         273 AA.
AC   Q2UPC2;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Gamma-glutamyl cyclotransferase aclK {ECO:0000303|PubMed:25302411};
DE            Short=GGCT aclK {ECO:0000305};
DE            EC=4.3.2.9 {ECO:0000250|UniProtKB:E9R9Y3};
DE   AltName: Full=Aspirochlorine biosynthesis protein K {ECO:0000303|PubMed:25302411};
GN   Name=aclK {ECO:0000303|PubMed:25302411}; ORFNames=AO090001000030;
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: Gamma-glutamyl cyclotransferase; part of the gene cluster
CC       that mediates the biosynthesis of aspirochlorine (or antibiotic
CC       A30641), an unusual halogenated spiro compound with distinctive
CC       antifungal properties due to selective inhibition of protein
CC       biosynthesis, and which is also active against bacteria, viruses, and
CC       murine tumor cells (PubMed:25302411). The non-ribosomal peptide
CC       synthetase (NRPS) aclP is responsible the formation of the
CC       diketopiperazine (DKP) core from the condensation of 2 phenylalanine
CC       residues (PubMed:25302411). One Phe residue is tailored into
CC       chlorotyrosine by hydroxylation and chlorination, whereas the second
CC       Phe undergoes an unprecedented C-C bond cleavage to be converted into
CC       glycine (PubMed:25302411). After formation of the DKP, sulfur is
CC       incorporated into the DKP by conjugation with glutathione by aclG,
CC       followed by its stepwise degradation to the thiol by aclI, aclJ and
CC       aclK, and the dithiol oxidation by aclT (PubMed:25302411). In addition,
CC       oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM
CC       and aclU) act as tailoring enzymes to produce the intermediate
CC       dechloroaspirochlorine (PubMed:25302411). Ultimately, chlorination of
CC       dechloroaspirochlorine by the halogenase aclH is the last step in the
CC       aspirochlorine pathway (PubMed:25302411).
CC       {ECO:0000269|PubMed:25302411}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline +
CC         an L-alpha-amino acid; Xref=Rhea:RHEA:20505, ChEBI:CHEBI:58402,
CC         ChEBI:CHEBI:59869, ChEBI:CHEBI:71304; EC=4.3.2.9;
CC         Evidence={ECO:0000250|UniProtKB:E9R9Y3};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25302411}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AP007154; BAE56593.1; -; Genomic_DNA.
DR   RefSeq; XP_001818595.1; XM_001818543.1.
DR   AlphaFoldDB; Q2UPC2; -.
DR   SMR; Q2UPC2; -.
DR   EnsemblFungi; BAE56593; BAE56593; AO090001000030.
DR   GeneID; 5990566; -.
DR   KEGG; aor:AO090001000030; -.
DR   VEuPathDB; FungiDB:AO090001000030; -.
DR   HOGENOM; CLU_030506_1_0_1; -.
DR   OMA; HDTIWAG; -.
DR   Proteomes; UP000006564; Chromosome 2.
DR   GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR017939; G-Glutamylcylcotransferase.
DR   PANTHER; PTHR12935; PTHR12935; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..273
FT                   /note="Gamma-glutamyl cyclotransferase aclK"
FT                   /id="PRO_0000441204"
SQ   SEQUENCE   273 AA;  30442 MW;  61D209FB7740CEF7 CRC64;
     MASSLELPKF EPDRDRLVWY LAYGSNLSSQ TFREDRQITP QAAVTITVPG WRLTLSSAGF
     PYREPSFASI VNVGSAGPTD EKHDGPCELP LHGTAYLITW SQWIKIVASE GGGIVYKEAL
     LRGQPIQPQD QQRWGAELSV LTLVSTMERW PEPRPSQRYM GLILDGARAA DFPASYIAQI
     RHKHPCYQPP STTWERIGAT LFLGFWTPVL TLLSLLTHAA ARAGPGDDGH VPEGVRALVR
     FAMFTMWWVH DLIWSRIWGR GDGLFPGAMQ LNG