ID A0A0W0C789_CANGB Unreviewed; 190 AA. AC A0A0W0C789; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 24-JUL-2024, entry version 28. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LLZZ01000107; KTB07688.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0W0C789; -. DR VEuPathDB; FungiDB:B1J91_G04147g; -. 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; IPR051884; Bis(5'-adenosyl)-TPase_reg. 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 //