ID   A0A0W0C789_CANGB        Unreviewed;       190 AA.
AC   A0A0W0C789;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   28-JUN-2023, entry version 26.
DE   RecName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000256|ARBA:ARBA00014605, ECO:0000256|RuleBase:RU366076};
DE            EC=3.6.1.29 {ECO:0000256|ARBA:ARBA00012377, ECO:0000256|RuleBase:RU366076};
GN   ORFNames=AO440_001656 {ECO:0000313|EMBL:KTB07688.1};
OS   Candida glabrata (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=5478 {ECO:0000313|EMBL:KTB07688.1, ECO:0000313|Proteomes:UP000054886};
RN   [1] {ECO:0000313|EMBL:KTB07688.1, ECO:0000313|Proteomes:UP000054886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=910700640 {ECO:0000313|EMBL:KTB07688.1};
RA   Haavelsrud O.E., Gaustad P.;
RT   "Draft genomes sequences of Candida glabrata isolates 1A, 1B, 2A, 2B, 3A
RT   and 3B.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves A-5'-PPP-5'A to yield AMP and ADP. Can cleave all
CC       dinucleoside polyphosphates, provided the phosphate chain contains at
CC       least 3 phosphates and that 1 of the 2 bases composing the nucleotide
CC       is a purine. Is most effective on dinucleoside triphosphates.
CC       Negatively regulates intracellular dinucleoside polyphosphate levels,
CC       which elevate following heat shock. {ECO:0000256|ARBA:ARBA00025241}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2
CC         H(+); Xref=Rhea:RHEA:13893, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58529, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC         EC=3.6.1.29; Evidence={ECO:0000256|ARBA:ARBA00001475,
CC         ECO:0000256|RuleBase:RU366076};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936,
CC         ECO:0000256|RuleBase:RU366076};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTB07688.1}.
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DR   EMBL; LLZZ01000107; KTB07688.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0C789; -.
DR   VEuPathDB; FungiDB:CAGL0G04147g; -.
DR   VEuPathDB; FungiDB:GVI51_G03993; -.
DR   VEuPathDB; FungiDB:GWK60_G03971; -.
DR   Proteomes; UP000054886; Unassembled WGS sequence.
DR   GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   CDD; cd01275; FHIT; 1.
DR   Gene3D; 3.30.428.10; HIT-like; 1.
DR   InterPro; IPR039383; FHIT.
DR   InterPro; IPR019808; Histidine_triad_CS.
DR   InterPro; IPR011146; HIT-like.
DR   InterPro; IPR036265; HIT-like_sf.
DR   PANTHER; PTHR46243; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR   PANTHER; PTHR46243:SF1; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR   Pfam; PF01230; HIT; 1.
DR   SUPFAM; SSF54197; HIT-like; 1.
DR   PROSITE; PS00892; HIT_1; 1.
DR   PROSITE; PS51084; HIT_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|RuleBase:RU366076};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU366076}.
FT   DOMAIN          5..117
FT                   /note="HIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51084"
FT   MOTIF           98..102
FT                   /note="Histidine triad motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT   ACT_SITE        100
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         93..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   SITE            117
FT                   /note="Important for induction of apoptosis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ   SEQUENCE   190 AA;  22284 MW;  6123A27F85AD2162 CRC64;
     MSGSTPIYFS KFLVTEQVFF RTRFSYALVN LKPITKGHVL VVPLRSQVVQ LSQLTPQENA
     DYFNTVQLIH QFMKWVYKAQ AVNIAIQDGP EAGQSVPHLH THIIPRYKEN NIGDKVYEHL
     DEWDLRRDEY MKARDMNEEG TNLRPDQDDV RIARSMEEMK KEVDFLKAQL EEFLSNHCDV
     KKWLATDARQ
//