AP4AH_STRA5
ID AP4AH_STRA5 Reviewed; 195 AA.
AC Q8DY32;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase, symmetrical {ECO:0000250|UniProtKB:Q2G297};
DE EC=3.6.1.41 {ECO:0000250|UniProtKB:Q2G297};
DE AltName: Full=Ap4A hydrolase {ECO:0000250|UniProtKB:Q2G297};
GN OrderedLocusNames=SAG1661 {ECO:0000312|EMBL:AAN00525.1};
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
RN [2] {ECO:0007744|PDB:2OGI}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH IRON AND GDP.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of conserved hypothetical protein TIGR00488
RT (NP_688652.1) from Streptococcus agalactiae 2603 at 1.85 A resolution.";
RL Submitted (JAN-2007) to the PDB data bank.
CC -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to
CC yield ADP. {ECO:0000250|UniProtKB:Q2G297}.
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:0000250|UniProtKB:Q2G297};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.2}.
CC -!- SIMILARITY: Belongs to the Ap4A hydrolase YqeK family. {ECO:0000305}.
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DR EMBL; AE009948; AAN00525.1; -; Genomic_DNA.
DR RefSeq; NP_688652.1; NC_004116.1.
DR RefSeq; WP_000221169.1; NC_004116.1.
DR PDB; 2OGI; X-ray; 1.85 A; A/B=1-195.
DR PDBsum; 2OGI; -.
DR SMR; Q8DY32; -.
DR STRING; 208435.SAG1661; -.
DR DNASU; 1014470; -.
DR EnsemblBacteria; AAN00525; AAN00525; SAG1661.
DR KEGG; sag:SAG1661; -.
DR PATRIC; fig|208435.3.peg.1670; -.
DR HOGENOM; CLU_089580_1_2_9; -.
DR OMA; ILTRNWA; -.
DR EvolutionaryTrace; Q8DY32; -.
DR Proteomes; UP000000821; 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 3D-structure; Hydrolase; Iron; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..195
FT /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT /id="PRO_0000454779"
FT DOMAIN 26..140
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT BINDING 29
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 29
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0007744|PDB:2OGI"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0007744|PDB:2OGI"
FT BINDING 59..62
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0007744|PDB:2OGI"
FT BINDING 91
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 117..118
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 135
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0007744|PDB:2OGI"
FT BINDING 141
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 178..183
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 24..44
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:2OGI"
FT TURN 58..63
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:2OGI"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 157..174
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:2OGI"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:2OGI"
SQ SEQUENCE 195 AA; 22317 MW; 9FA9B1C06451A488 CRC64;
MTYKDYTGLD RTELLSKVRH MMSDKRFNHV LGVERAAIEL AERYGYDKEK AGLAALLHDY
AKELSDDEFL RLIDKYQPDP DLKKWGNNIW HGLVGIYKIQ EDLAIKDQDI LAAIAKHTVG
SAQMSTLDKI VYVADYIEHN RDFPGVEEAR ELAKVDLNKA VAYETARTVA FLASKAQPIY
PKTIETYNAY IPYLD
