AP4AH_ALKHC
ID AP4AH_ALKHC Reviewed; 187 AA.
AC Q9KD90;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=BH1327 {ECO:0000312|EMBL:BAB05046.1};
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2] {ECO:0007744|PDB:2O08}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON AND DGDP.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of hypothetical protein (NP_242193.1) from Bacillus
RT halodurans at 1.90 A resolution.";
RL Submitted (NOV-2006) 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; BA000004; BAB05046.1; -; Genomic_DNA.
DR PIR; G83815; G83815.
DR RefSeq; WP_010897494.1; NC_002570.2.
DR PDB; 2O08; X-ray; 1.90 A; A/B=1-187.
DR PDBsum; 2O08; -.
DR SMR; Q9KD90; -.
DR STRING; 272558.10173943; -.
DR EnsemblBacteria; BAB05046; BAB05046; BAB05046.
DR KEGG; bha:BH1327; -.
DR eggNOG; COG1713; Bacteria.
DR HOGENOM; CLU_089580_1_2_9; -.
DR OMA; ILTRNWA; -.
DR OrthoDB; 1433958at2; -.
DR EvolutionaryTrace; Q9KD90; -.
DR Proteomes; UP000001258; 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..187
FT /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT /id="PRO_0000454777"
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:0000305|Ref.2"
FT BINDING 21
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0007744|PDB:2O08"
FT BINDING 50
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0007744|PDB:2O08"
FT BINDING 51..54
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0007744|PDB:2O08"
FT BINDING 83
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 109..110
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 127
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0007744|PDB:2O08"
FT BINDING 133
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 170..175
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|Ref.2"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:2O08"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2O08"
FT HELIX 16..36
FT /evidence="ECO:0007829|PDB:2O08"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:2O08"
FT TURN 50..55
FT /evidence="ECO:0007829|PDB:2O08"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:2O08"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2O08"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2O08"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:2O08"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:2O08"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:2O08"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:2O08"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:2O08"
FT HELIX 149..166
FT /evidence="ECO:0007829|PDB:2O08"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:2O08"
SQ SEQUENCE 187 AA; 21521 MW; 43B6583ADA32B73E CRC64;
MNRGKALQLV KPHLTEHRYQ HTIGVMETAI DLAKLYGADQ QKAELAAIFH DYAKFRDKNE
MRTLIREKLS QQDILFYGDE LLHAPCGAYY VREEVGIEDE DVLQAIRFHT TGRPNMSLLE
KIIFLADYIE PNRQFPGVEK VRTQAKTDLN GAIISSLVNT ITFLLKKNQP IYPDTLATYN
QLLLEQK
