PBCD_EMENI
ID PBCD_EMENI Reviewed; 266 AA.
AC A0A1U8QXK4; C8VN88; Q5BCY5;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Glutathione S-transferase AN1595 {ECO:0000303|PubMed:22506079};
DE EC=2.5.1.- {ECO:0000305|PubMed:22506079};
DE AltName: Full=Pimaradiene biosynthesis cluster protein AN1595 {ECO:0000303|PubMed:22506079};
GN ORFNames=AN1595, ANIA_01595;
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 FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=22506079; DOI=10.1371/journal.pone.0035450;
RA Bromann K., Toivari M., Viljanen K., Vuoristo A., Ruohonen L.,
RA Nakari-Setaelae T.;
RT "Identification and characterization of a novel diterpene gene cluster in
RT Aspergillus nidulans.";
RL PLoS ONE 7:e35450-e35450(2012).
RN [4]
RP FUNCTION.
RX PubMed=27098256; DOI=10.1007/s00253-016-7517-5;
RA Bromann K., Toivari M., Viljanen K., Ruohonen L., Nakari-Setaelae T.;
RT "Engineering Aspergillus nidulans for heterologous ent-kaurene and gamma-
RT terpinene production.";
RL Appl. Microbiol. Biotechnol. 100:6345-6359(2016).
CC -!- FUNCTION: Glutathione S-transferase; part of the gene cluster that
CC mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene
CC (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-
CC CoA reductase AN1593 functions in the mevalonate pathway, which
CC produces isoprenoid precursors (PubMed:22506079, PubMed:27098256). The
CC geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the
CC formation of GGPP, the precursor for diterpenes (PubMed:22506079,
CC PubMed:27098256). Lastly, the pimaradiene synthase pbcA performs the 2
CC cyclization steps that convert GGPP to ent-pimara-8(14),15-diene
CC (PubMed:22506079, PubMed:27098256). The putative roles of the remaining
CC cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear
CC (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione
CC S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably
CC function as decorative enzymes (Probable). It is possible that in
CC biological conditions the compound is oxidized to ent-pimara-8(14),15-
CC dien-19-oic acid, which is a bioactive diterpene compound predominant
CC in many plant extracts (Probable). {ECO:0000269|PubMed:22506079,
CC ECO:0000269|PubMed:27098256, ECO:0000305|PubMed:22506079}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:22506079}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor pbcR. {ECO:0000269|PubMed:22506079}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; AACD01000025; EAA64302.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF85182.1; -; Genomic_DNA.
DR RefSeq; XP_659199.1; XM_654107.1.
DR AlphaFoldDB; A0A1U8QXK4; -.
DR SMR; A0A1U8QXK4; -.
DR STRING; 162425.CADANIAP00008228; -.
DR EnsemblFungi; CBF85182; CBF85182; ANIA_01595.
DR EnsemblFungi; EAA64302; EAA64302; AN1595.2.
DR GeneID; 2874629; -.
DR KEGG; ani:AN1595.2; -.
DR VEuPathDB; FungiDB:AN1595; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_3_2_1; -.
DR OMA; EAWPIKV; -.
DR OrthoDB; 1341490at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Transferase.
FT CHAIN 1..266
FT /note="Glutathione S-transferase AN1595"
FT /id="PRO_0000450842"
FT DOMAIN 43..123
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 128..259
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
FT BINDING 93
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q4WB03"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4WB03"
FT BINDING 107
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q4WB03"
FT BINDING 108
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q4WB03"
FT BINDING 143
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q4WB03"
SQ SEQUENCE 266 AA; 29717 MW; AEC2A191AAF4DD6D CRC64;
MNTLNAPRNP TRHPAMTADT LVDAPALPHQ NGSTEEKLKE RGSFGKLYTY KRSPRALGIQ
AVAKSIGLEL EQVELQPANG VPDFYWNLNP LGKTPTFVGA DGLVLTECMA IALHVTNEDS
TTTLLGSSSL DFVQIIRWIS FTNTDVVTRM ASWVRPLIGY TPYSKEEVLK AQQQTTQAIG
VFEDSLRDRK YLVGDRLTLA DIMCVSLVSF GFAQIFDKEW REAFPYFSGW YMMVMHLPIM
KAVVEEVPFV EEGLPNAPPT EPFRAP
