AP4AH_STAA8
ID AP4AH_STAA8 Reviewed; 194 AA.
AC Q2G297;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase, symmetrical {ECO:0000305};
DE EC=3.6.1.41 {ECO:0000269|PubMed:32152217};
DE AltName: Full=Ap4A hydrolase {ECO:0000305};
DE AltName: Full=Symmetrically cleaving Ap4A hydrolase {ECO:0000303|PubMed:32152217};
GN Name=yqeK {ECO:0000303|PubMed:32152217};
GN OrderedLocusNames=SAOUHSC_01696 {ECO:0000312|EMBL:ABD30770.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=32152217; DOI=10.1128/jb.00053-20;
RA Minazzato G., Gasparrini M., Amici A., Cianci M., Mazzola F., Orsomando G.,
RA Sorci L., Raffaelli N.;
RT "Functional characterization of COG1713 (YqeK) as a novel diadenosine
RT tetraphosphate hydrolase family.";
RL J. Bacteriol. 202:e00053-e00053(2020).
CC -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to
CC yield ADP (PubMed:32152217). Can also hydrolyze Ap3A, Ap5A, Ap4G, Ap4U
CC and Gp4G, always releasing ADP or GDP as one of the products, but it
CC exhibits a marked preference for Ap4A, which is mainly exerted at the
CC substrate affinity level (PubMed:32152217).
CC {ECO:0000269|PubMed:32152217}.
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:0000269|PubMed:32152217};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:32152217}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 uM for Ap4A {ECO:0000269|PubMed:32152217};
CC KM=21.5 uM for Ap5A {ECO:0000269|PubMed:32152217};
CC KM=19.7 uM for Ap4G {ECO:0000269|PubMed:32152217};
CC KM=17.6 uM for Ap4U {ECO:0000269|PubMed:32152217};
CC KM=68.0 uM for Gp4G {ECO:0000269|PubMed:32152217};
CC Note=kcat is 107 sec(-1) with Ap4A as substrate. kcat is 32 sec(-1)
CC with Ap5A as substrate. kcat is 210 sec(-1) with Ap4G as substrate.
CC kcat is 324 sec(-1) with Ap4U as substrate. kcat is 1002 sec(-1) with
CC Gp4G as substrate. {ECO:0000269|PubMed:32152217};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:32152217}.
CC -!- SIMILARITY: Belongs to the Ap4A hydrolase YqeK family. {ECO:0000305}.
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DR EMBL; CP000253; ABD30770.1; -; Genomic_DNA.
DR RefSeq; WP_001019324.1; NZ_LS483365.1.
DR RefSeq; YP_500206.1; NC_007795.1.
DR AlphaFoldDB; Q2G297; -.
DR SMR; Q2G297; -.
DR STRING; 1280.SAXN108_1618; -.
DR EnsemblBacteria; ABD30770; ABD30770; SAOUHSC_01696.
DR GeneID; 3921808; -.
DR KEGG; sao:SAOUHSC_01696; -.
DR PATRIC; fig|93061.5.peg.1545; -.
DR eggNOG; COG1713; Bacteria.
DR HOGENOM; CLU_089580_1_1_9; -.
DR OMA; ILTRNWA; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR005249; YqeK.
DR Pfam; PF01966; HD; 1.
DR SMART; SM00471; HDc; 1.
DR TIGRFAMs; TIGR00488; TIGR00488; 1.
DR PROSITE; PS51831; HD; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Iron; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..194
FT /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT /id="PRO_0000454778"
FT DOMAIN 18..132
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT BINDING 21
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 21
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 50
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 51..54
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 83
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 109..110
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 127
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 133
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 172..177
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
SQ SEQUENCE 194 AA; 22464 MW; 15F2A27F5B5D55FF CRC64;
MNIEKAKRLA KEKLPEKRYN HSLRVAETAI KLAEIYDGDT SKVELAGVLH DFCKYDDLGK
MYQIVRQYEL GNDLLSYGSE ILHGPVCAAI MEHEYGINDE EVLMAIKYHT TGRQQMTKTE
KLIFIADYIE PGRTIPGVDD IRDMAYNQGS LDKTIYEISK RTVLFLIQKD ITVYNKTIDC
LNYYNYSDER IKDD
