ID   TASG_HAPIR              Reviewed;         325 AA.
AC   A0A0F7CUE9;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Aminotransferase tasG {ECO:0000303|PubMed:25885659};
DE            EC=2.6.1.- {ECO:0000305|PubMed:25885659};
DE   AltName: Full=Tetramic acid Sch210971/2 biosynthesis cluster protein G {ECO:0000303|PubMed:25885659};
GN   Name=tasG {ECO:0000303|PubMed:25885659};
OS   Hapsidospora irregularis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Hapsidospora.
OX   NCBI_TaxID=95324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX   PubMed=25885659; DOI=10.1021/acs.orglett.5b00715;
RA   Kakule T.B., Zhang S., Zhan J., Schmidt E.W.;
RT   "Biosynthesis of the tetramic acids Sch210971 and Sch210972.";
RL   Org. Lett. 17:2295-2297(2015).
CC   -!- FUNCTION: Aminotransferase; part of the gene cluster that mediates the
CC       biosynthesis of the tetramic acids Sch210971 and Sch210972, potential
CC       anti-HIV fungal natural product that contain a decalin core
CC       (PubMed:25885659). The PKS module of tasS together with the
CC       enoylreductase tasC catalyze the formation of the polyketide unit which
CC       is then conjugated to 4-hydroxyl-4-methyl glutamate (HMG) by the
CC       condensation domain of the tasS NRPS module (PubMed:25885659). One
CC       unique structural feature of Sch210971 and Sch210972 is the tetramic
CC       acid motif proposed to be derived from the non-proteinogenic amino acid
CC       HMG, by a Dieckmann-type condensation catalyzed by the reductase domain
CC       of tasS (PubMed:25885659). The aldolase tasA catalyzes the aldol
CC       condensation of 2 molecules of pyruvic acid to yield the intermediate
CC       4-hydroxyl-4-methyl-2-oxoglutarate (HMOG), which can then be
CC       stereoselectively transaminated, may be by tasG, to form HMG
CC       (PubMed:25885659). The Diels-Alderase tas3 then uses the Dieckmann
CC       product of tasS as substrate and catalyzes the Diels-Alder
CC       cycloaddition to form the decalin ring of Sch210971 and Sch210972
CC       (PubMed:25885659). {ECO:0000269|PubMed:25885659}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q93ZN9};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:25885659}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q93ZN9}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; KP835202; AKG54862.1; -; Genomic_DNA.
DR   SMR; A0A0F7CUE9; -.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR000796; Asp_trans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11879; PTHR11879; 3.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..325
FT                   /note="Aminotransferase tasG"
FT                   /id="PRO_0000453348"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         89..90
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   BINDING         143
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O84395,
FT                   ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         174
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   BINDING         203..205
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   BINDING         214
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   MOD_RES         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
SQ   SEQUENCE   325 AA;  35713 MW;  A5A3D798C1CA33D1 CRC64;
     MFFDSVTNGP EDVMYQVKAA CDSDNDPSKI DLGVGTYRNE DGDYHELDVL KEIATVQTIS
     GTGAIHIGAM FLARSATDVL PHVYVGTPTW GNYQPLLRLA GLEMRTYNHY LSQTGRVDFA
     SVLSAIRTTP RGSTFILQGC CHNPTAADFS REQWDIVVAE MESHGHLPFF DIAYQGLGEG
     VDEDVYGVRL CADKGMEMVV CQSFAKNFGL YGERCGALHV VCTSDDVAAR VKDQLRCLIR
     WEFSSSPAYG ARLVNLVLSD ARAEEQCLLP LSKTQCQELQ NKFRIYAVPN GRITMSGLSQ
     GNIDYAARAI DAVVRSGLEA REPTG