ID E1TA82_BURSG Unreviewed; 311 AA.
AC E1TA82;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase, symmetrical {ECO:0000256|HAMAP-Rule:MF_00199};
DE EC=3.6.1.41 {ECO:0000256|HAMAP-Rule:MF_00199};
DE AltName: Full=Ap4A hydrolase {ECO:0000256|HAMAP-Rule:MF_00199};
DE AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase {ECO:0000256|HAMAP-Rule:MF_00199};
DE AltName: Full=Diadenosine tetraphosphatase {ECO:0000256|HAMAP-Rule:MF_00199};
GN Name=apaH {ECO:0000256|HAMAP-Rule:MF_00199};
GN OrderedLocusNames=BC1003_0745 {ECO:0000313|EMBL:ADN56734.1};
OS Burkholderia sp. (strain CCGE1003).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN56734.1};
RN [1] {ECO:0000313|EMBL:ADN56734.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN56734.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT "Complete sequence of chromosome1 of Burkholderia sp. CCGE1003.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield
CC ADP. {ECO:0000256|ARBA:ARBA00003413, ECO:0000256|HAMAP-Rule:MF_00199}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2
CC H(+); Xref=Rhea:RHEA:24252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58141, ChEBI:CHEBI:456216; EC=3.6.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00001682, ECO:0000256|HAMAP-
CC Rule:MF_00199};
CC -!- SIMILARITY: Belongs to the Ap4A hydrolase family.
CC {ECO:0000256|ARBA:ARBA00005419, ECO:0000256|HAMAP-Rule:MF_00199}.
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DR EMBL; CP002217; ADN56734.1; -; Genomic_DNA.
DR AlphaFoldDB; E1TA82; -.
DR STRING; 640512.BC1003_0745; -.
DR KEGG; bgf:BC1003_0745; -.
DR eggNOG; COG0639; Bacteria.
DR HOGENOM; CLU_056184_1_0_4; -.
DR GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; IEA:UniProtKB-UniRule.
DR CDD; cd07422; MPP_ApaH; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR HAMAP; MF_00199; ApaH; 1.
DR InterPro; IPR004617; ApaH.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR NCBIfam; TIGR00668; apaH; 1.
DR PANTHER; PTHR42850:SF11; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE [SYMMETRICAL]; 1.
DR PANTHER; PTHR42850; METALLOPHOSPHOESTERASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF000903; B5n-ttraPtase_sm; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00199};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..311
FT /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003151472"
FT DOMAIN 34..172
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
SQ SEQUENCE 311 AA; 33847 MW; 3C5EBF62865C33D9 CRC64;
MRRRVYRTAN ILSMTPSNAP SFASSTVQQR PAPLAFGDLQ GCRTPFQRLL AKAAPPADAP
LWFAGDLINR GTESLATLRD IIALGERAVP VLGNHDLHLL SVSAGIRKSK KGDTIDEILA
APDAADLLEW VRHRPIAHYE NGMLMVHAGV LPQWDVNLTL ELADELQRAL RAPNWKETLA
GLYGNEPSLW TPDLKGIERL RVTCSALTRV RFCNAEGAMD FSSSGGLNAA PPGCMPWFDV
PWRKTADVTV VFGHWAALGL TLRDNLIGLD SGCVWGEKLS AVRLAPNPAE RTLTQVECEN
CRARGGNATA L
//
