ID I3J4V0_ORENI Unreviewed; 149 AA.
AC I3J4V0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 08-NOV-2023, entry version 51.
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:ENSONIP00000003890.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000003890.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000003890.2}
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 RefSeq; XP_003446525.1; XM_003446477.3.
DR RefSeq; XP_019214078.1; XM_019358533.1.
DR AlphaFoldDB; I3J4V0; -.
DR Ensembl; ENSONIT00000003891.2; ENSONIP00000003890.2; ENSONIG00000003104.2.
DR GeneID; 100702722; -.
DR KEGG; onl:100702722; -.
DR CTD; 2272; -.
DR GeneTree; ENSGT00510000047967; -.
DR InParanoid; I3J4V0; -.
DR OMA; HSYGFVN; -.
DR OrthoDB; 1365844at2759; -.
DR Proteomes; UP000005207; Linkage group LG5.
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; 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:UP000005207}.
FT DOMAIN 1..110
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT REGION 117..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 95..99
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT ACT_SITE 97
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 90..93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT SITE 115
FT /note="Important for induction of apoptosis"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ SEQUENCE 149 AA; 16928 MW; E259B1B88A91321A CRC64;
MATLRFGQHL IKLSAVFLQT ELSFALVNRK PVVPGHVLVC PLRPVERFRD LRPDELADLF
STTQRVANLV EKHFSATSIT IAIQDGPEAG QTVKHVHVHV LPRKAGDFQH NDSIYDELQN
HDQEDKDIPS KWRSEEEMAA EASDLRKQL
//