ALNF_EMENI
ID ALNF_EMENI Reviewed; 428 AA.
AC A0A1U8QYW8; C8VJR2; Q5AR60;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Acetyltransferase sirH {ECO:0000303|PubMed:30339758};
DE EC=2.3.1.- {ECO:0000305|PubMed:30339758};
DE AltName: Full=Asperlin biosynthesis cluster protein F {ECO:0000303|PubMed:30339758};
GN Name=alnF {ECO:0000303|PubMed:30339758}; ORFNames=AN9220.2;
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, DISRUPTION PHENOTYPE, FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=30339758; DOI=10.1021/acschembio.8b00679;
RA Grau M.F., Entwistle R., Chiang Y.M., Ahuja M., Oakley C.E., Akashi T.,
RA Wang C.C.C., Todd R.B., Oakley B.R.;
RT "Hybrid transcription factor engineering activates the silent secondary
RT metabolite gene cluster for (+)-asperlin in Aspergillus nidulans.";
RL ACS Chem. Biol. 13:3193-3205(2018).
CC -!- FUNCTION: Acetyltransferase; part of the gene cluster that mediates the
CC biosynthesis of asperlin, a polyketide showing anti-inflammatory,
CC antitumor and antibiotic activities (PubMed:30339758). The first step
CC of the asperlin biosynthesis is the production of the intermediate
CC 2,4,6-octatrienoic acid by the highly redusing polyketide synthase alnA
CC with cleavage of the PKS product by the esterase alnB
CC (PubMed:30339758). 2,4,6-octatrienoic acid is further converted to
CC asperlin via several steps involving the remaining enzymes from the
CC cluster (PubMed:30339758). {ECO:0000269|PubMed:30339758}.
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:30339758}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is controlled by the asperlin biosynthesis
CC cluster-specific transcription factor alnR.
CC {ECO:0000269|PubMed:30339758}.
CC -!- DISRUPTION PHENOTYPE: Fully eliminates the production of asperlin.
CC {ECO:0000269|PubMed:30339758}.
CC -!- SIMILARITY: Belongs to the wax synthase family. {ECO:0000305}.
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DR EMBL; AACD01000170; EAA61511.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF82295.1; -; Genomic_DNA.
DR RefSeq; XP_682489.1; XM_677397.1.
DR AlphaFoldDB; A0A1U8QYW8; -.
DR EnsemblFungi; CBF82295; CBF82295; ANIA_09220.
DR EnsemblFungi; EAA61511; EAA61511; AN9220.2.
DR GeneID; 2868003; -.
DR KEGG; ani:AN9220.2; -.
DR eggNOG; ENOG502SIV2; Eukaryota.
DR HOGENOM; CLU_032731_1_1_1; -.
DR OMA; FFMDAIF; -.
DR OrthoDB; 606079at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR InterPro; IPR044851; Wax_synthase.
DR InterPro; IPR032805; Wax_synthase_dom.
DR PANTHER; PTHR31595; PTHR31595; 1.
DR Pfam; PF13813; MBOAT_2; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Glycoprotein; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..428
FT /note="Acetyltransferase sirH"
FT /id="PRO_0000445949"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 428 AA; 48595 MW; 23FC45D348EE110C CRC64;
MADYVIQNLT SNLQAMQYAY SSREEMPVWA TKLLTPIFMA VAVLTTLPPP GPLRVIVGLT
AFTSLWLHVL THWVSGPAFF MDAIFMISIT VRWLLMFVAG TPEIDYHQTT QSGTTITHKG
TKDSSTLRQG LTKLRWSVEL WSCWRGQGWN FVDQHLPRGA ERTQSRWEFL VSNAGRVLLN
QYISDLVRKY AFCALWPAQV DAHVDFSSLP LLNRHGLVAL QLIRDSLMLD SEYRKASILF
VGLHLSTPDR WPSLFGNMRD LYTVRNFWGR VWHQIFRQIF TRCGDIVANA LNAQKGTLLY
KYSRLYVGFL VSGVQHYACA LLIPSAEYGW GMFWQMPAYA AVVTVEDILK YYGREAGIQD
GNFVRFLGYI WTAYWMTLIY ALPVGFVSDI GGFTGDGNFQ LSDPCVSCSS TSIPVSGFES
IDLEFGLW
