ID   TASH_HAPIR              Reviewed;         324 AA.
AC   A0A0F7CUE8;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Dioxygenase tasH {ECO:0000303|PubMed:25885659};
DE            EC=1.-.-.- {ECO:0000305|PubMed:25885659};
DE   AltName: Full=Tetramic acid Sch210971/2 biosynthesis cluster protein H {ECO:0000303|PubMed:25885659};
DE   Flags: Precursor;
GN   Name=tasH {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, CATALYTIC ACTIVITY, AND
RP   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: Dioxygenase; 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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P24197};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P24197};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P24197}.
CC   -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening
CC       dioxygenase family. {ECO:0000305}.
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DR   EMBL; KP835202; AKG54857.1; -; Genomic_DNA.
DR   SMR; A0A0F7CUE8; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   CDD; cd07363; 45_DOPA_Dioxygenase; 1.
DR   InterPro; IPR014436; Extradiol_dOase_DODA.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   Pfam; PF02900; LigB; 1.
DR   PIRSF; PIRSF006157; Doxgns_DODA; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Metal-binding; Oxidoreductase; Signal; Zinc.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..324
FT                   /note="Dioxygenase tasH"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5012994845"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P24197"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P24197"
FT   BINDING         284
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P24197"
SQ   SEQUENCE   324 AA;  35021 MW;  CF08352586DF1738 CRC64;
     MRSMSLWMLI GPVTGIATWA SLRYAATTTT SSTAAASTRM GLAPVIALSH GGGPLPLLGD
     PGHKSIIHSL SHRIPKILSL NDPDRRPRAI ILITAHWSTA APTISGAANP DLIYDYYGFP
     PETYELKYPA RGDPGIAAEA AAAFRAEGLG DVVVDPGRGW DHGVFVPMTL VRPEADIPIV
     QMSVLASEDP TSHLRMGRAL RALRAENIAI VGSGFASFHN LRAMMAMRSS AGSRNPEGAR
     IQAISREWNS ALTDVVDKNP WQGLEGWRSL PGADLMHPPR GGEHFMPLIA CAGAAHEEEK
     VRWYTDEYLG VDIYTYYWGG SDVE