ID A0A2I3GNE0_NOMLE Unreviewed; 150 AA.
AC A0A2I3GNE0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000256|RuleBase:RU366076};
DE EC=3.6.1.29 {ECO:0000256|RuleBase:RU366076};
GN Name=FHIT {ECO:0000313|Ensembl:ENSNLEP00000032826.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000032826.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000032826.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000032826.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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|RuleBase:RU366076};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU366076};
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DR EMBL; ADFV01077688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01077689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01077690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01077691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01077692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01077693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01077694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01077695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01077696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01077697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3GNE0; -.
DR STRING; 61853.ENSNLEP00000032826; -.
DR Ensembl; ENSNLET00000039344.1; ENSNLEP00000032826.1; ENSNLEG00000033239.1.
DR GeneTree; ENSGT00510000047967; -.
DR InParanoid; A0A2I3GNE0; -.
DR OMA; HSYGFVN; -.
DR Proteomes; UP000001073; Chromosome 21.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; IEA:Ensembl.
DR GO; GO:0047627; F:adenylylsulfatase activity; IEA:Ensembl.
DR GO; GO:0047352; F:adenylylsulfate-ammonia adenylyltransferase activity; IEA:Ensembl.
DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0015964; P:diadenosine triphosphate catabolic process; IEA:Ensembl.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:Ensembl.
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; PTHR46981; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR PANTHER; PTHR46981: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073}.
FT DOMAIN 2..109
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT MOTIF 94..98
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT ACT_SITE 96
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT SITE 114
FT /note="Important for induction of apoptosis"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ SEQUENCE 150 AA; 17142 MW; 893E78CC09429BBC CRC64;
MSFRFGQHLI KPSAVFLKTE LSFAFVNRKP VVPGHVLVCP LRPVERFRDL RTDEVADLFQ
ATQRVGTVVE KHFHGTSVTF SMQDGPEAGQ TVKHVHVHVL PRKAGDFHRN DSIYEELQKH
DKEEEDSPAS CRSEEEMAAE AVALRVYFQR
//