ID A0A2G5BD43_COERN Unreviewed; 168 AA.
AC A0A2G5BD43;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000256|RuleBase:RU366076};
DE EC=3.6.1.29 {ECO:0000256|RuleBase:RU366076};
GN ORFNames=COEREDRAFT_80968 {ECO:0000313|EMBL:PIA16930.1};
OS Coemansia reversa (strain ATCC 12441 / NRRL 1564).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX NCBI_TaxID=763665 {ECO:0000313|EMBL:PIA16930.1, ECO:0000313|Proteomes:UP000242474};
RN [1] {ECO:0000313|EMBL:PIA16930.1, ECO:0000313|Proteomes:UP000242474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1564 {ECO:0000313|EMBL:PIA16930.1,
RC ECO:0000313|Proteomes:UP000242474};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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; KZ303497; PIA16930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5BD43; -.
DR STRING; 763665.A0A2G5BD43; -.
DR OrthoDB; 1365844at2759; -.
DR Proteomes; UP000242474; 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; 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:UP000242474}.
FT DOMAIN 7..115
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT MOTIF 100..104
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT ACT_SITE 102
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 95..98
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT SITE 120
FT /note="Important for induction of apoptosis"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ SEQUENCE 168 AA; 18764 MW; 5D72AB20A92D12ED CRC64;
MALPVARTFW FGPLTIPLAQ LFLLTKHTLG IVNIKPIRPG HVLVVTRRQV ARFNELSQDE
IADLFAQGQR VSKIIERLYS ADGLTLCIQD GSAAGQTVPH VHLHVIPRHI GDFANNDDIY
SVLDGTGKVP LQTHIDNEQR RPRSLADMTA EAEILRREIG DWDSETVT
//
