LNBC_ASPFN
ID LNBC_ASPFN Reviewed; 503 AA.
AC B8NWW3;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Cytochrome P450 monooxygenase lnbC {ECO:0000303|PubMed:23281040};
DE EC=1.-.-.- {ECO:0000305|PubMed:23281040};
DE AltName: Full=Lnb diastereomeric piperazines biosynthesis cluster protein C {ECO:0000303|PubMed:23281040};
GN Name=lnbC {ECO:0000303|PubMed:23281040}; ORFNames=AFLA_121500;
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, 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 lnb 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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ963485; EED45921.1; -; Genomic_DNA.
DR RefSeq; XP_002384857.1; XM_002384816.1.
DR AlphaFoldDB; B8NWW3; -.
DR SMR; B8NWW3; -.
DR STRING; 5059.CADAFLAP00012722; -.
DR EnsemblFungi; EED45921; EED45921; AFLA_121500.
DR VEuPathDB; FungiDB:AFLA_121500; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_11_1; -.
DR OMA; CYPDANG; -.
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 Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..503
FT /note="Cytochrome P450 monooxygenase lnbC"
FT /id="PRO_0000446079"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 446
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 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 503 AA; 56609 MW; 69FB8AFD27D272EF CRC64;
MAARLLSSVS LTDVVLLLSS VWIAVHLVLA AYNVYLHPLR RYPGPKLAAA SQLLNVYHVL
KGDNCKWTAQ LHEKYGTVVR IGPNELSYIS PSANQTIFGG RPKEDKVFEK NPVAYLQGNG
DISNIFFARF HDHNRLRKLM APAFSETAVR EQEATIQGYT NQLIAALRNR SGQAAYPDAK
GVVNIIPWLH FILFDVLTRL SFGDPIGCLD RADYHPWVSV IFKAIIHSTY TQAAHRLAPY
QWILKHFIPN DMTANYEAHL EFTRKQLDQR QQVKEEPVAR ADFSSFMLKG MSPDELFDNV
NIVITAGGET TASTISSSLY YLVHNPSSYE RLTKEIRDTF SAEGEITLAA VAALPYLKAV
IQEAMRIHPP VPIGLFRVAP AAGAFIDGQW VPGNTWVSVA NLAASRSPTY WRDPERFTPE
RWLGDAKYES DVREASAPFS IGTRNCIGLN LANANMRIIL ARLLWNFDFE AQPDNIDPHE
LDEYGIWETK PLNLKIKERV QTT
