LAEA_ASPOR
ID LAEA_ASPOR Reviewed; 498 AA.
AC Q2ULA2; A7BG61;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Secondary metabolism regulator laeA {ECO:0000305};
DE AltName: Full=Methyltransferase laeA {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:C8VQG9};
DE AltName: Full=Velvet complex subunit laeA {ECO:0000305};
GN Name=laeA {ECO:0000303|PubMed:21897021}; ORFNames=AO090003000489;
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 [GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RA Yamada O.;
RT "Functional analysis of laeA gene from Aspergillus oryzae.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21897021; DOI=10.1271/bbb.110235;
RA Oda K., Kobayashi A., Ohashi S., Sano M.;
RT "Aspergillus oryzae laeA regulates kojic acid synthesis genes.";
RL Biosci. Biotechnol. Biochem. 75:1832-1834(2011).
RN [4]
RP FUNCTION.
RX PubMed=22083274; DOI=10.1007/s00253-011-3657-9;
RA Sakai K., Kinoshita H., Nihira T.;
RT "Heterologous expression system in Aspergillus oryzae for fungal
RT biosynthetic gene clusters of secondary metabolites.";
RL Appl. Microbiol. Biotechnol. 93:2011-2022(2012).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=23729383; DOI=10.1128/ec.00003-13;
RA Kawauchi M., Nishiura M., Iwashita K.;
RT "Fungus-specific sirtuin HstD coordinates secondary metabolism and
RT development through control of LaeA.";
RL Eukaryot. Cell 12:1087-1096(2013).
CC -!- FUNCTION: Methyltransferase that performs automethylation (By
CC similarity). No other methyl-accepting substrate has been identified
CC yet (By similarity). Component of the velvet transcription factor
CC complex that acts as a global regulator for secondary metabolite gene
CC expression (PubMed:21897021, PubMed:22083274, PubMed:23729383).
CC Controls the expression of the kojic acid gene cluster, producing a
CC secondary metabolite used as a skin-lightening agent, an antioxidant,
CC and an antibiotic (PubMed:21897021). {ECO:0000250|UniProtKB:C8VQG9,
CC ECO:0000269|PubMed:21897021, ECO:0000269|PubMed:22083274,
CC ECO:0000269|PubMed:23729383}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionyl-[protein] + S-adenosyl-L-methionine = S-adenosyl-
CC L-homocysteine + S-methyl-L-methionyl-[protein];
CC Xref=Rhea:RHEA:60560, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:15592,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:142742; Evidence={ECO:0000250|UniProtKB:C8VQG9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60561;
CC Evidence={ECO:0000250|UniProtKB:C8VQG9};
CC -!- SUBUNIT: Component of the heterotrimeric velvet complex composed of
CC laeA, veA and velB; VeA acting as a bridging protein between laeA and
CC velB (By similarity). {ECO:0000250|UniProtKB:C8VQG9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VQG9}.
CC -!- INDUCTION: Expression is negatively regulated by hstD
CC (PubMed:23729383). {ECO:0000269|PubMed:23729383}.
CC -!- DISRUPTION PHENOTYPE: Impairs kojik acid production (PubMed:21897021).
CC {ECO:0000269|PubMed:21897021}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC methyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE57663.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB267276; BAF74528.1; -; Genomic_DNA.
DR EMBL; AP007155; BAE57663.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q2ULA2; -.
DR STRING; 510516.Q2ULA2; -.
DR PRIDE; Q2ULA2; -.
DR HOGENOM; CLU_010595_2_0_1; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 2.
PE 2: Evidence at transcript level;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Sporulation; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..498
FT /note="Secondary metabolism regulator laeA"
FT /id="PRO_0000435745"
SQ SEQUENCE 498 AA; 57535 MW; 328EFD13E3CF0E6C CRC64;
MSSEKQPFYE ENGRMYHAYR KGVYMLPCDE QEQDRLDIFH KLFTVARVSD GLMYAPHPRN
GRFLDLGCGT GIWAIDVANK YPDAFVVGVD LAPIQPSNHP KNCEFYAPFD FESPWAMGED
SWDLIHLQMM FGNGQTGQRL PAMASPPHDS YYSQSLASSR SRNNSDAMDI YAITDRDPPA
REPSGYSQWY RNGSPSVNSI HSKSSEKQPF YEENGRMYHA YRKGVYMLPC DEQEQDRLDI
FHKLFTVARV SDGLMYAPHP RNGRFLDLGC GTGIWAIDVA NKYPDAFVVG VDLAPIQPSN
HPKNCEFYAP FDFESPWAMG EDSWDLIHLQ MGCGSVMGWP NLYRRIFAHL RPGAWFEQVE
IDFEPRCDDR PLEGLAIRQW YQYLKQATQD AMRPINHNSR DTIRDLQEAG FTDIDHQMVG
LPLNPWHQDE HERKVARWYN LAVSESIESL SMAPFSRIFN WDLDRIRRIS SEVKSEAFNK
EIHAYNILHI YQARKPAN
