TASK_HAPIR
ID TASK_HAPIR Reviewed; 981 AA.
AC A0A0F7GG06;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Amidohydrolase tasK {ECO:0000303|PubMed:25885659};
DE EC=3.5.4.- {ECO:0000305|PubMed:25885659};
DE AltName: Full=Tetramic acid Sch210971/2 biosynthesis cluster protein K {ECO:0000303|PubMed:25885659};
GN Name=tasK {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], AND FUNCTION.
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: Amidohydrolase; 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=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P25524};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P25524};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P25524};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC {ECO:0000305}.
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DR EMBL; KP835202; AKG54855.1; -; Genomic_DNA.
DR SMR; A0A0F7GG06; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Iron; Manganese; Membrane; Metal-binding;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..981
FT /note="Amidohydrolase tasK"
FT /id="PRO_0000453358"
FT TRANSMEM 40..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 187
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25524"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25524"
FT BINDING 189
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25524"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25524"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 891
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 981 AA; 105554 MW; 438F23D5A5BEBAD1 CRC64;
MDDQKGPLPP YTPTATAPPP ASMRQRRPPG RRRALRRSRT VRVLALACLA FVVLAQWKQL
WRGERKAPPY LSVDKLNDNL ETCRKLRVRP QDPAGPGRSK NDRYLDGGGK PTLIRNALIW
TGEPVPGTSD EDARAGVGWA WWLGDVLVER GLITKVDNKM PASEVPEDAI IYDAEGRRLT
SGIVDMHSHA GVSPLPGLNG NDDTNEASDN ITPWARSIDG LFPLDPQIQV IKSGGVTSSL
ILPGSANNIG GEAFLIKHAV GRHDGRPELS AASMLADPDR TWRYMKMACG ENAKRVHGSR
TTRPVTRMGE SYDFRRAFER ASQLVRRQDD WCDRAGEVGV GSMDEYLPED LEWEALGAAL
RGQVHVNAHC YTVNDLEAMV DHSNEFEFPI RAFHHAHQAH LVPEILNRTW GGRPPALAIF
ADNMYYKAEA YIGTPSAGKM LYDQGLTPIY VSDNPVLNAQ HVVLEAAKGF HYGLPYHAAL
ASVTTAPADT LGMGQRLGKI KAGFDADIVV WDSDPLGVGA APVQVWIDGT AQFDDPVVLS
KPHARAEKDT VVVPDAPPPV VVEEPVEVAD VLFRGVTRVL LDEHDVSAED GASLNVAIRG
GRISCIGECA DEFRVAIDAG VGVVTLGNGH LHKTFVGVGG TLGLNEIDGE SKTGNGKNPK
TFTRAVDGLL LGGKKLRAAH HAGVTRAISA PRFKGGGNTH HGTSVGIVTS ARTSLDAGAI
FGNGDVAVHY TLDLSVRGGD DESYSAAFGS LREKLIRAGV HGGKEKEVGA EEVGAEEEEE
EEEKAFLRRV LASEMVLALT INSADGIATA LRIKDEVDKK QQKQQQQQQQ QQQQQHGTSS
GIRMAIIGGA EAYLVAEHLA AANVGVILSP LQSYGETWDA RRALPGAPLT NGTNIDRLLD
AGVKVGIGLK EDWEVRDLAL AAGTAYENGG GRLTGRQALD LVGRNVLEIL GVEEEEETPG
ATMGESGHFV VLLIINMFCG L
