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LNAC_ASPFN
ID   LNAC_ASPFN              Reviewed;         524 AA.
AC   B8NU01;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Cytochrome P450 monooxygenase lnaC {ECO:0000303|PubMed:23281040};
DE            EC=1.-.-.- {ECO:0000305|PubMed:23281040};
DE   AltName: Full=Lna diastereomeric piperazines biosynthesis cluster protein C {ECO:0000303|PubMed:23281040};
GN   Name=lnaC {ECO:0000303|PubMed:23281040}; ORFNames=AFLA_101720;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2]
RP   IDENTIFICATION, FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=23281040; DOI=10.1002/anie.201207456;
RA   Forseth R.R., Amaike S., Schwenk D., Affeldt K.J., Hoffmeister D.,
RA   Schroeder F.C., Keller N.P.;
RT   "Homologous NRPS-like gene clusters mediate redundant small-molecule
RT   biosynthesis in Aspergillus flavus.";
RL   Angew. Chem. Int. Ed. 52:1590-1594(2013).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the lna gene cluster
CC       that mediates the biosynthesis of diastereomeric piperazines. Lna and
CC       lnb clusters encode sets of enzymes that produce overlapping sets of
CC       previously undescribed metabolites such as piperazinomycin-like
CC       metabolites or morpholine (PubMed:23281040). The lna and lnb
CC       biosynthetic pathways appear to be part of a signaling network that
CC       controls the formation of sclerotia, a resilient overwintering
CC       structure (PubMed:23281040). One primary function of the non-canonical
CC       nonribosomal peptide synthetases lnaA and lnbA consists in the
CC       reduction of L-tyrosine (PubMed:23281040). The presence in the clusters
CC       of tailoring enzymes such as the oxidoreductases lnaB, lnbB, lnaE or
CC       lnbE, as well as of the cytochrome P450 monooxygenases lnaC, lnaD, or
CC       lnbC, might explain formation of various diastereomeric piperazines
CC       (PubMed:23281040). {ECO:0000269|PubMed:23281040}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:23281040}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is regulated by a complex signaling network which
CC       may include cross-pathway interactions mediated by sensing of the
CC       cluster final products or shared biosynthetic intermediates.
CC       {ECO:0000269|PubMed:23281040}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; EQ963484; EED46508.1; -; Genomic_DNA.
DR   RefSeq; XP_002384044.1; XM_002384003.1.
DR   AlphaFoldDB; B8NU01; -.
DR   SMR; B8NU01; -.
DR   EnsemblFungi; EED46508; EED46508; AFLA_101720.
DR   VEuPathDB; FungiDB:AFLA_101720; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_022195_9_2_1; -.
DR   OMA; AFERIMY; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..524
FT                   /note="Cytochrome P450 monooxygenase lnaC"
FT                   /id="PRO_0000446078"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         471
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"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   524 AA;  58898 MW;  8628B1FE24B1635A CRC64;
     MIGEQYTSII TGFKSALAVS CIAVSLFLLS PWIAYARLPS SIKSPIKAKG PLSALRACLN
     EISAGAKTST RGYELYSKKG QSFAMLNINF RPQVILPPEH VRWLVTQPED ILSHAKASDD
     ADALGYIWPL FDASALHSFS KVLQIDLTRN VTQTEKDVLE EVQHIMDELV GQTESWKEVN
     MVQAFERIMY QATQRVYVGL PLCRDSTYMG YVKGYARSLG TAMVFAAQLT PWPLRQVTAL
     LAGLPVYYYV LRVRSYLSPL FKERMERLKE KGGTQDDNLE GEPRNLITWM SDGVLSGVGP
     KSISPSEMVT WLGILALLPT DNLWTTCTNV LLDLLSSESE HAYLHTIREE ARTVFASSKE
     SGKPVSHGLH HIDSAIRESL RMNSLSPRSL HRQVVRRGGV VLPDGQKVPT GTWLCVLSGN
     IQRDEDYYED AQTYKPFRFV PKLTEAGGDK APLLPLTNEK YLTFGYGRHA CPGRWFSFQV
     MKIVIAYILA NYDIQPLEKR PDNIVFADLN IPHLSHIIRI KRMT
 
 
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