TERH_ASPTN
ID TERH_ASPTN Reviewed; 340 AA.
AC Q0D1P7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=NAD-dependent epimerase/dehydratase terH {ECO:0000303|PubMed:24816227};
DE EC=1.1.1.- {ECO:0000305|PubMed:24816227};
DE AltName: Full=Terrein biosynthesis cluster protein terH {ECO:0000303|PubMed:24816227};
GN Name=terH {ECO:0000303|PubMed:24816227}; ORFNames=ATEG_00137;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24816227; DOI=10.1016/j.chembiol.2014.03.010;
RA Zaehle C., Gressler M., Shelest E., Geib E., Hertweck C., Brock M.;
RT "Terrein biosynthesis in Aspergillus terreus and its impact on
RT phytotoxicity.";
RL Chem. Biol. 21:719-731(2014).
RN [3]
RP INDUCTION.
RX PubMed=25852654; DOI=10.3389/fmicb.2015.00184;
RA Gressler M., Hortschansky P., Geib E., Brock M.;
RT "A new high-performance heterologous fungal expression system based on
RT regulatory elements from the Aspergillus terreus terrein gene cluster.";
RL Front. Microbiol. 6:184-184(2015).
CC -!- FUNCTION: NAD-dependent epimerase/dehydratase; part of the gene cluster
CC that mediates the biosynthesis of terrein, a fungal metabolite with
CC ecological, antimicrobial, antiproliferative, and antioxidative
CC activities (PubMed:24816227). The first step in the pathway is
CC performed by the polyketide synthase terA that produces 4-hydroxy-6-
CC methylpyranon (4-HMP), orsellinic acid (OA), and 2,3-dehydro-6-
CC hydroxymellein (2,3-dehydro-6-HM) by condensing acetyl-CoA with two,
CC three, or four malonyl-CoA units, respectively (PubMed:24816227). 4-HMP
CC and OA are not pathway intermediates, but are rather shunt or side
CC products (PubMed:24816227). 2,3-dehydro-6-HM is further converted to 6-
CC hydroxymellein (6-HM) by the 6-hydroxymellein synthase terB
CC (PubMed:24816227). The monooxygenases terC and terD, the multicopper
CC oxidase terE and the Kelch-like protein terF are then involved in the
CC transformation of 6-HM to terrein (PubMed:24816227). Even if they are
CC co-regulated with the other terrein cluster genes, terH and terI seem
CC to be dispensable for terrein production; whereas one or both of the 2
CC transporters terG and terJ are probably required for efficient
CC secretion of metabolites (PubMed:24816227).
CC {ECO:0000269|PubMed:24816227}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is under the control of the terrein cluster-
CC specific transcription factor terR (PubMed:25852654).
CC {ECO:0000269|PubMed:25852654}.
CC -!- DISRUPTION PHENOTYPE: Reduces, but does not abolish, the production of
CC terrein (PubMed:24816227). {ECO:0000269|PubMed:24816227}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476594; EAU38783.1; -; Genomic_DNA.
DR RefSeq; XP_001210223.1; XM_001210223.1.
DR AlphaFoldDB; Q0D1P7; -.
DR SMR; Q0D1P7; -.
DR STRING; 33178.CADATEAP00005726; -.
DR EnsemblFungi; EAU38783; EAU38783; ATEG_00137.
DR GeneID; 4354894; -.
DR VEuPathDB; FungiDB:ATEG_00137; -.
DR eggNOG; KOG1502; Eukaryota.
DR HOGENOM; CLU_007383_9_2_1; -.
DR OMA; PYEPERC; -.
DR OrthoDB; 848823at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..340
FT /note="NAD-dependent epimerase/dehydratase terH"
FT /id="PRO_0000437630"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 340 AA; 37864 MW; 67750922CF90D6A7 CRC64;
MTVSSSIVPP GGLVLVTGVT GFIGSYIANG LLELGYRVRG TVRSSEKATW VTKALTKRNP
SANFEAVIVP DQNAPGVWEA VLKDVDGIAH VAGDVSFGPD PTKVITPSVE ALRRLLEAAK
KEPSVKRFVF TSSDQAASNR STTREILINE DTWNEEAIEA AWRPPPYEAE RGWDVYSALK
AQVEKEMWRF SREEKPSFVV NSVLPTYTIG AIFDEQQAGS TAKWLLDFYK DPSKDGFMRG
FGSSYYVYVG DVALLHIGAL TLEEVQNKRL LAFAGRFNFN SWLEVFRKHD PSKPWPEDDP
TQALDTRRVN GETELYILKQ FGKDGWTSFE DSALKVLESP
