ID B8BIS6_ORYSI Unreviewed; 152 AA.
AC B8BIS6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000256|RuleBase:RU366076};
DE EC=3.6.1.29 {ECO:0000256|RuleBase:RU366076};
GN ORFNames=OsI_34902 {ECO:0000313|EMBL:EEC67561.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000313|EMBL:EEC67561.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EEC67561.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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; CM000136; EEC67561.1; -; Genomic_DNA.
DR AlphaFoldDB; B8BIS6; -.
DR STRING; 39946.B8BIS6; -.
DR EnsemblPlants; BGIOSGA034697-TA; BGIOSGA034697-PA; BGIOSGA034697.
DR Gramene; BGIOSGA034697-TA; BGIOSGA034697-PA; BGIOSGA034697.
DR HOGENOM; CLU_056776_7_1_1; -.
DR OMA; DAIYGMM; -.
DR Proteomes; UP000007015; Chromosome 11.
DR GO; GO:0047627; F:adenylylsulfatase activity; IEA:UniProt.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007015}.
FT DOMAIN 36..107
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT MOTIF 92..96
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT ACT_SITE 94
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT SITE 112
FT /note="Important for induction of apoptosis"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ SEQUENCE 152 AA; 17588 MW; 9B7151208597AD78 CRC64;
MEAAYKFGPY KIDAREVFHS TPLSYAMVNL RPLLPVCPKR EVKRFADLSS NEISDLWVTA
KEVGIRLEQY HKASSLTFAI QDGPQAGQTV PHVHIHVIPR KKGDFEKNDE IYDAIDVKER
ELKEKLDLDI ERKDRTMEEM AHEANEYRGL FS
//
