ATNJ_EMENI
ID ATNJ_EMENI Reviewed; 348 AA.
AC Q5AV04; A0A1U8QXP8; C8V3Y1;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Aminotransferase atnJ {ECO:0000303|PubMed:26563584};
DE EC=2.6.1.- {ECO:0000305|PubMed:26563584};
DE AltName: Full=Aspercryptin biosynthesis cluster protein J {ECO:0000303|PubMed:26563584};
GN Name=atnJ {ECO:0000303|PubMed:26563584}; ORFNames=ANIA_07876;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP IDENTIFICATION OF THE CLUSTER.
RX PubMed=23248299; DOI=10.1073/pnas.1205532110;
RA Andersen M.R., Nielsen J.B., Klitgaard A., Petersen L.M., Zachariasen M.,
RA Hansen T.J., Blicher L.H., Gotfredsen C.H., Larsen T.O., Nielsen K.F.,
RA Mortensen U.H.;
RT "Accurate prediction of secondary metabolite gene clusters in filamentous
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E99-E107(2013).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=27310134; DOI=10.1021/acschembio.6b00398;
RA Henke M.T., Soukup A.A., Goering A.W., McClure R.A., Thomson R.J.,
RA Keller N.P., Kelleher N.L.;
RT "New aspercryptins, lipopeptide natural products, revealed by HDAC
RT inhibition in Aspergillus nidulans.";
RL ACS Chem. Biol. 11:2117-2123(2016).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=26563584; DOI=10.1002/anie.201507097;
RA Chiang Y.M., Ahuja M., Oakley C.E., Entwistle R., Asokan A., Zutz C.,
RA Wang C.C., Oakley B.R.;
RT "Development of genetic dereplication strains in Aspergillus nidulans
RT results in the discovery of aspercryptin.";
RL Angew. Chem. Int. Ed. 55:1662-1665(2016).
CC -!- FUNCTION: Aminotransferase; part of the gene cluster that mediates the
CC biosynthesis of aspercryptins, linear lipopeptides built from six amino
CC acids including 2 highly unusual and nonproteogenic amino acids, 2-
CC amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol)
CC (PubMed:23248299, PubMed:27310134, PubMed:26563584). The core structure
CC of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol
CC (PubMed:27310134). The first step of aspercryptin biosynthesis is the
CC generation of the fatty acid precursors, octanoic and dodecanoic acids,
CC by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584).
CC The fatty acid precursors are likely transformed into the corresponding
CC alpha-amino fatty acids in three steps (PubMed:27310134,
CC PubMed:26563584). First, they are hydroxylated by the cytochrome P450
CC monooxygenase atnE, then oxidized to the corresponding alpha-keto acids
CC by the NAD(P)-dependent oxidoreductase atnD, and finally converted to
CC the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH
CC or atnJ (PubMed:27310134, PubMed:26563584). the alpha-amino fatty
CC acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized,
CC activated, and covalently tethered to the NRPS atnA by its fourth and
CC sixth adenylation domains (PubMed:27310134). The second module of atnA
CC is the Thr module and contains an epimerase (E) domain responsible for
CC the epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally,
CC despite atnA having only one epimerase domain, the first amino acid of
CC aspercryptin A1 is D-Ser, suggesting that serine is either loaded
CC directly as D-Ser on the first module or that the epimerase domain in
CC the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134).
CC After condensation of the hexapeptide of aspercryptin, the C-terminal
CC reductase (TE) domain might be involved in the reductive release and
CC production of the aldehyde hexapeptide (PubMed:26563584). Further
CC reduction would generate aspercryptins (PubMed:27310134,
CC PubMed:26563584). The variety of aspercryptins produced reflects the
CC flexibiliy of the atnA NRPS, allowing incorporation of alanine instead
CC of serine, valine for isoleucine, and a C10 fatty amino alcohol instead
CC of the C12 version (PubMed:27310134). AtnB seems to be involved in the
CC selectivity for Ile versus Val by the third module (PubMed:26563584).
CC Moreover, type B, C and D aspercryptins have an additional N-terminal
CC cichorine, acetyl and propionyl group respectively (PubMed:27310134).
CC {ECO:0000269|PubMed:23248299, ECO:0000269|PubMed:26563584,
CC ECO:0000269|PubMed:27310134}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P19938};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:26563584}.
CC -!- INDUCTION: Expression is positively regulated by the aspercryptin
CC cluser-specific transcription factor atnN (PubMed:27310134).
CC {ECO:0000269|PubMed:27310134}.
CC -!- DISRUPTION PHENOTYPE: Eliminates approximately 70% of aspercryptin
CC production (PubMed:26563584). {ECO:0000269|PubMed:26563584}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BN001302; CBF73436.1; -; Genomic_DNA.
DR EMBL; AACD01000135; EAA59530.1; -; Genomic_DNA.
DR RefSeq; XP_681145.1; XM_676053.1.
DR AlphaFoldDB; Q5AV04; -.
DR SMR; Q5AV04; -.
DR STRING; 162425.CADANIAP00003892; -.
DR EnsemblFungi; CBF73436; CBF73436; ANIA_07876.
DR EnsemblFungi; EAA59530; EAA59530; AN7876.2.
DR GeneID; 2869017; -.
DR KEGG; ani:AN7876.2; -.
DR eggNOG; KOG0975; Eukaryota.
DR HOGENOM; CLU_031922_1_0_1; -.
DR InParanoid; Q5AV04; -.
DR OMA; LKWSDQA; -.
DR OrthoDB; 853728at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central.
DR GO; GO:0009081; P:branched-chain amino acid metabolic process; IEA:InterPro.
DR CDD; cd01557; BCAT_beta_family; 1.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005786; B_amino_transII.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
DR PANTHER; PTHR42825; PTHR42825; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR PIRSF; PIRSF006468; BCAT1; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
PE 2: Evidence at transcript level;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..348
FT /note="Aminotransferase atnJ"
FT /id="PRO_0000444132"
FT BINDING 79
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 216
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT MOD_RES 180
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P19938"
SQ SEQUENCE 348 AA; 38402 MW; E93B242468FEE461 CRC64;
MSTFPAEPRS DIVNGHVESD FNYQTGTWSE PVFVQDHYLK VHGLAPGLNY GQQVFEGMKA
YRDPNGQIQI FRPTDHALRM QRSCDAVSIP SIPESLFWAS VNLAVAKNSE FVPPHASEAA
MYIRPLAFGS GGWMPVAAGP QYKFVVYALP FCAYHGTLPV DAVVLEELDR AAPLGVGNVK
VGGNYAPVLK WSDKARKEGF GITLHLDSKT RGEIDEFSTS GFVGIKYTES GGEKGYTLVV
PNSQCIIKSV TSTSVVEVAR SLGWRVEVRP IPYDELEFFD EVLAVGTAAM ITSIRSITHR
SKDQVFRYKT SDEPGSACEK LSRHLKGIQK GDEKDTFGWL KRVEEVTV
