HNT2_YEAS6
ID HNT2_YEAS6 Reviewed; 206 AA.
AC B5VGI4;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase;
DE EC=3.6.1.29;
DE AltName: Full=AP3A hydrolase;
DE Short=AP3Aase;
DE AltName: Full=Diadenosine 5',5'''-P1,P3-triphosphate hydrolase;
DE AltName: Full=Dinucleosidetriphosphatase;
DE AltName: Full=Hit family protein 2;
GN Name=HNT2; Synonyms=APH1; ORFNames=AWRI1631_45190;
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631;
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
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 (By similarity). {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Divalent metal cations. Mn(2+) is the preferred ion.
CC {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Mitochondrion {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDZ72959.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; ABSV01000513; EDZ72959.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; B5VGI4; -.
DR SMR; B5VGI4; -.
DR Proteomes; UP000008988; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd01275; FHIT; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR039383; FHIT.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR Pfam; PF01230; HIT; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Mitochondrion; Nucleotide-binding; Nucleus.
FT CHAIN 1..206
FT /note="Bis(5'-adenosyl)-triphosphatase"
FT /id="PRO_0000392105"
FT DOMAIN 3..115
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT REGION 143..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 96..100
FT /note="Histidine triad motif"
FT COMPBIAS 144..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 206 AA; 23542 MW; 4143F7371805B378 CRC64;
MNKPIYFSKF LVTEQVFYKS KYTYALVNLK PIVPGHVLIV PLRTTVLNLS DLTMPESQDY
FKTLQLIHRF IKWQYKADSI NVAIQDGPEA GQSVPHLHTH IIPRYKINNV GDLIYDKLDH
WDGNGTLTDW QGRRDEYLGV GGRQARKNNS TSATVDGDEL SQGPNVLKPD SQRKVRALTE
MKKEAEDLQA RLEEFVSSDP GLTQWL
