ID   TERI_ASPTN              Reviewed;         197 AA.
AC   Q0D1P8;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Lactoylglutathione lyase-like protein terB {ECO:0000305};
DE            EC=4.4.-.- {ECO:0000305};
DE   AltName: Full=Terrein biosynthesis cluster protein terB {ECO:0000303|PubMed:24816227};
DE   Flags: Precursor;
GN   Name=terI {ECO:0000303|PubMed:24816227}; ORFNames=ATEG_00136;
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: Lactoylglutathione lyase-like protein; part of the gene
CC       cluster that mediates the biosynthesis of terrein, a fungal metabolite
CC       with 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   -!- 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 glyoxalase I family. {ECO:0000305}.
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DR   EMBL; CH476594; EAU38782.1; -; Genomic_DNA.
DR   RefSeq; XP_001210222.1; XM_001210222.1.
DR   AlphaFoldDB; Q0D1P8; -.
DR   EnsemblFungi; EAU38782; EAU38782; ATEG_00136.
DR   GeneID; 4354893; -.
DR   VEuPathDB; FungiDB:ATEG_00136; -.
DR   HOGENOM; CLU_1383886_0_0_1; -.
DR   OrthoDB; 1717119at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.180.10; -; 1.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR037523; VOC.
DR   SUPFAM; SSF54593; SSF54593; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Lyase; Metal-binding; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..197
FT                   /note="Lactoylglutathione lyase-like protein terB"
FT                   /id="PRO_5004170688"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   197 AA;  21341 MW;  6B2FF4094A858AC0 CRC64;
     MARFAVLQLL LPLAAGLTGA SFPAQIPTIL EEPDTPHYAV HHTVVSASSL SESLKFYVDG
     LGLDIIRNYN FQGDLTTLFG TNTSVLPGYF LGDTTSVYNG TDGVIYLVEF PDAKKIPTDE
     SDPPNTGLFL TSFWMGDKLN ATLDRLDRLG MGGKPHIATF SFGSEPLATY ATVRDPDGAR
     VLLVSRPYIN SIGKQRP