ID U3BGU4_VIBPR Unreviewed; 270 AA.
AC U3BGU4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 ECO:0000313|EMBL:GAD68879.1};
GN ORFNames=VPR01S_20_00590 {ECO:0000313|EMBL:GAD68879.1};
OS Vibrio proteolyticus NBRC 13287.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD68879.1, ECO:0000313|Proteomes:UP000016570};
RN [1] {ECO:0000313|EMBL:GAD68879.1, ECO:0000313|Proteomes:UP000016570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD68879.1,
RC ECO:0000313|Proteomes:UP000016570};
RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287.";
RL Submitted (SEP-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD68879.1}.
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DR EMBL; BATJ01000020; GAD68879.1; -; Genomic_DNA.
DR RefSeq; WP_021706847.1; NZ_BATJ01000020.1.
DR AlphaFoldDB; U3BGU4; -.
DR STRING; 1219065.VPR01S_20_00590; -.
DR eggNOG; COG0639; Bacteria.
DR Proteomes; UP000016570; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000016570}.
FT DOMAIN 1..151
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
SQ SEQUENCE 270 AA; 30939 MW; 90268F2FBC12FCED CRC64;
MSTYIVGDIQ GCFDELQALL TQAGFCADND HLWLAGDLVA RGPKSLETLR FVRDLGDNAT
VVLGNHDLHL LAVSLGIHKV KKKDQTQPIF DAPDRDELLA WLRQQPLLAE HDQFVMAHAG
ISPQWDLDTA RQCAREVEHV LRSEHWPWLI EHMYSNTPDF WQPTLSGLER YRYIINAYTR
MRFCLPDGRL DMACKLPPNE VSPQELMPWF RLPQRIQLAK PVLFGHWAAL EGYQGESVIG
LDTGCVWGGS LTMLRWEDQR WFHQPALTTA
//