APAH_SHIFL
ID APAH_SHIFL Reviewed; 280 AA.
AC Q83SQ2; Q7C3B6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 119.
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};
GN OrderedLocusNames=SF0046, S0048;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN41712.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP15592.1; -; Genomic_DNA.
DR RefSeq; NP_706005.1; NC_004337.2.
DR RefSeq; WP_000257186.1; NZ_WPGW01000005.1.
DR PDB; 2DFJ; X-ray; 2.72 A; A/B=1-280.
DR PDBsum; 2DFJ; -.
DR AlphaFoldDB; Q83SQ2; -.
DR SMR; Q83SQ2; -.
DR STRING; 198214.SF0046; -.
DR EnsemblBacteria; AAN41712; AAN41712; SF0046.
DR EnsemblBacteria; AAP15592; AAP15592; S0048.
DR GeneID; 1024575; -.
DR GeneID; 66671661; -.
DR KEGG; sfl:SF0046; -.
DR KEGG; sfx:S0048; -.
DR PATRIC; fig|198214.7.peg.55; -.
DR HOGENOM; CLU_056184_2_0_6; -.
DR OMA; INAFTRM; -.
DR OrthoDB; 900869at2; -.
DR EvolutionaryTrace; Q83SQ2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..280
FT /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT /id="PRO_0000198011"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:2DFJ"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2DFJ"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2DFJ"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:2DFJ"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:2DFJ"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:2DFJ"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:2DFJ"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 129..144
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:2DFJ"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2DFJ"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:2DFJ"
FT TURN 216..220
FT /evidence="ECO:0007829|PDB:2DFJ"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:2DFJ"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2DFJ"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2DFJ"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:2DFJ"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:2DFJ"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:2DFJ"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:2DFJ"
SQ SEQUENCE 280 AA; 31283 MW; BD6560C73336B6BB CRC64;
MATYLIGDVH GCYDELIALL HKVEFTPGKD TLWLTGDLVA RGPGSLDVLR YVKSLGDSVR
LVLGNHDLHL LAVFAGISRN KPKDRLTPLL EAPDADELLN WLRRQPLLQI DEEKKLVMAH
AGITPQWDLQ TAKECARDVE AVLSSDSYPF FLDAMYGDMP NNWSPELRGL GRLRFITNAF
TRMRFCFPNG QLDMYSKESP EEAPAPLKPW FAIPGPVAEE YSIAFGHWAS LEGKGTPEGI
YALDTGCCWG GSLTCLRWED KQYFVQPSNR HKDLGEAAAS
