LNAD_ASPFN
ID LNAD_ASPFN Reviewed; 511 AA.
AC B8NU02;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Cytochrome P450 monooxygenase lnaD {ECO:0000303|PubMed:23281040};
DE EC=1.-.-.- {ECO:0000305|PubMed:23281040};
DE AltName: Full=Ferulate-5-hydroxylase {ECO:0000303|PubMed:23281040};
DE AltName: Full=Lna diastereomeric piperazines biosynthesis cluster protein D {ECO:0000303|PubMed:23281040};
GN Name=lnaD {ECO:0000303|PubMed:23281040}; ORFNames=AFLA_101730;
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; EED46509.1; -; Genomic_DNA.
DR RefSeq; XP_002384045.1; XM_002384004.1.
DR AlphaFoldDB; B8NU02; -.
DR SMR; B8NU02; -.
DR EnsemblFungi; EED46509; EED46509; AFLA_101730.
DR VEuPathDB; FungiDB:AFLA_101730; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_022195_9_2_1; -.
DR OMA; FAHIFKV; -.
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..511
FT /note="Cytochrome P450 monooxygenase lnaD"
FT /id="PRO_0000446080"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 458
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 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 511 AA; 58344 MW; 2C72DA6D122B5E11 CRC64;
MAASTTAQIL VVSLGLLIFV LLCPWFGYLR LPSSMRWWPS IPSGPLSALR LSLKEYSGSR
SSEDGYKAFS KKAELFAICN PSFYPQVLLP PEQIPWLLSQ PENVLSHEKA NEDVHALPFL
APAFDNYDHL ELIRAIRTDL TRNIPNTEDA FLDELRHTTN EVLGAPGDNA WKEVNLTVAL
DSIIFGICLR LFFGVSLSRN RTFVYYVKIF TRVTGAMMLF VSQLVPWPLK PVVGIVAGFP
IYYYWVRLII YLYPTFKERI QCLRTKKETP PADMVTWMVD LAISQNPTRK VHISSLIVRL
TLIVFLPVDV LIAMTDNFFL DLLSSDPDRK YYNALRQEAE AAFTNRDKTQ PISQSMPYME
STIRESLRLS PLSDRMLSRR VVHKGGITLP DGQFLPRGTW LAVAAVGVHR DERTYEDPDE
YRPFRFLSED TETKEAKAML VPVTSEKFLA FGHGRHSCPG RWFAAHAMKL IIGYILVNYD
IEPLEKRPVN SVVGQTIIPQ LDVKIRVRRR E
