APAH_SALPB
ID APAH_SALPB Reviewed; 282 AA.
AC A9MYM2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase, symmetrical {ECO:0000255|HAMAP-Rule:MF_00199};
DE EC=3.6.1.41 {ECO:0000255|HAMAP-Rule:MF_00199};
DE AltName: Full=Ap4A hydrolase {ECO:0000255|HAMAP-Rule:MF_00199};
DE AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00199};
DE AltName: Full=Diadenosine tetraphosphatase {ECO:0000255|HAMAP-Rule:MF_00199};
GN Name=apaH {ECO:0000255|HAMAP-Rule:MF_00199}; OrderedLocusNames=SPAB_00113;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield
CC ADP. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00199};
CC -!- SIMILARITY: Belongs to the Ap4A hydrolase family. {ECO:0000255|HAMAP-
CC Rule:MF_00199}.
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DR EMBL; CP000886; ABX65556.1; -; Genomic_DNA.
DR RefSeq; WP_000257211.1; NC_010102.1.
DR AlphaFoldDB; A9MYM2; -.
DR SMR; A9MYM2; -.
DR KEGG; spq:SPAB_00113; -.
DR PATRIC; fig|1016998.12.peg.107; -.
DR HOGENOM; CLU_056184_2_0_6; -.
DR OMA; INAFTRM; -.
DR BioCyc; SENT1016998:SPAB_RS00440-MON; -.
DR Proteomes; UP000008556; Chromosome.
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 Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF000903; B5n-ttraPtase_sm; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR00668; apaH; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..282
FT /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT /id="PRO_1000077719"
SQ SEQUENCE 282 AA; 31431 MW; B5B701E39CA7869E CRC64;
MATYLIGDVH GCYDELIALL QQVEFTPDTD TLWLTGDLVA RGPGSLDVLR YVKSLGNSVR
LVLGNHDLHL LAVFAGISRN KPKDRLTPLL EAPDADELLN WLRRQPLLQV DEEKKLVMAH
AGITPQWDLQ TAKECARDVE AVLSSDSYPF FLDAMYGDMP NNWSPELSGL ARLRFITNAF
TRMRYCFPNG QLDMYSKASP ENAPAPLKPW FAIPGPVSEA YSIAFGHWAS LEGKGTPEGI
YALDTGCCWG GELTCLRWED KQYFVQPSNR QMDMGEGEAV NA