ACLB_ASPOR
ID ACLB_ASPOR Reviewed; 527 AA.
AC Q2UPB7;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cytochrome P450 monooxygenase aclB {ECO:0000303|PubMed:25302411};
DE EC=1.-.-.- {ECO:0000305|PubMed:25302411};
DE AltName: Full=Aspirochlorine biosynthesis protein B {ECO:0000303|PubMed:25302411};
GN Name=aclB {ECO:0000303|PubMed:25302411}; ORFNames=AO090001000035;
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: Cytochrome P450 monooxygenase; 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=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25302411}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AP007154; BAE56598.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UPB7; -.
DR SMR; Q2UPB7; -.
DR EnsemblFungi; BAE56598; BAE56598; AO090001000035.
DR HOGENOM; CLU_022195_0_2_1; -.
DR OMA; WLASTID; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 1.10.630.10; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..527
FT /note="Cytochrome P450 monooxygenase aclB"
FT /id="PRO_0000441195"
FT BINDING 466
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 527 AA; 59406 MW; A73914A81DAC3AD2 CRC64;
MASESSIPLY DCLIIGGGIA GLSSALSLVR TLHTAVVFDE GIHRNDQAPH LATVPTWDSQ
DPKRFRDAAK LNILSKYSTV EFANVKLEKF NKALGKPFLT KVFGHDYVVL PSKYFDDIKR
ASPQSLSFFQ ALSDGLNMEA SVGHLYASTT EIDVVVKHLN PRLTQLTPLL CDEAEYAIER
EVGALPDWKK FNVSNLIAAI VHRTTNRILV GKELCRNEEY LAITTKFSRS LFISGIFWNF
VRLGPLRKLV AWLTIGLHLR DRNAAAKVLL PHVLARRQEK EAGVDVATKY PDALQWTIDT
APSFPGDDEP LHQVYHMLHL TFAASSASGV GVTQCLLNVL AYPEYLEPLR DEISTVVARH
GGWTDKALSQ MALLDSFIRE TMRLHPAGSF MDDHFRFHDG LTLPKGTNII APALAIHYDP
DNYEDAHRFD GFRFARYRQK QGENHRWLAS TIDQKFLQFG YGNHACPGRF YAIRKIKLVL
AKLIMDYDFK WAQPRPVHDR PEDFAIEAQL VAAPDAEILI RSRNLSN
