(data stored in ACNUC30567 zone)

HOGENOM: ACCPU_4_PE900

ID   ACCPU_4_PE900                        STANDARD;      PRT;   195 AA.
AC   ACCPU_4_PE900; C7RPN2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Non-canonical purine NTP pyrophosphatase; EC=3.6.1
DE   19;AltName: Full=Non-standard purine NTP pyrophosphatase;AltName:
DE   Full=Nucleoside-triphosphate diphosphatase;AltName:
DE   Full=Nucleoside-triphosphate pyrophosphatase; (ACCPU_4.PE900).
GN   OrderedLocusNames=CAP2UW1_0938;
OS   CANDIDATUS ACCUMULIBACTER PHOSPHATIS CLADE IIA STR. UW-1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=522306;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACCPU_4.PE900.
CC       Candidatus Accumulibacter phosphatis clade IIA str. UW-1, complete geno
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C7RPN2_ACCPU
CC   -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine
CC       nucleotides such as XTP and ITP/dITP to their respective
CC       monophosphate derivatives. Might exclude non-canonical purines
CC       from DNA precursor pool, thus preventing their incorporation into
CC       DNA and avoiding chromosomal lesions (By similarity).
CC   -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
CC       nucleotide + diphosphate.
CC   -!- COFACTOR: Binds 1 divalent metal cation ion per subunit; can use
CC       either magnesium or manganese (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family.
CC   -!- GENE_FAMILY: HOG000293319 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C7RPN2; -.
DR   EMBL; CP001715; ACV34275.1; -; Genomic_DNA.
DR   RefSeq; YP_003166204.1; NC_013194.1.
DR   ProteinModelPortal; C7RPN2; -.
DR   STRING; C7RPN2; -.
DR   GeneID; 8403074; -.
DR   GenomeReviews; CP001715_GR; CAP2UW1_0938.
DR   KEGG; app:CAP2UW1_0938; -.
DR   ProtClustDB; PRK00120; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:HAMAP.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:HAMAP.
DR   HAMAP; MF_01405; Nucleoside_triphosp; 1; -.
DR   InterPro; IPR002637; Ham1p-like.
DR   InterPro; IPR020922; Nucleoside-triphosphatase.
DR   PANTHER; PTHR11067; Ham1p_like; 1.
DR   Pfam; PF01725; Ham1p_like; 1.
DR   TIGRFAMs; TIGR00042; TIGR00042; 1.
DR   HOGENOMDNA; ACCPU_4.PE900; -.
KW   Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding.
SQ   SEQUENCE   195 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKLVLASNNA KKLKELDAIL APLGWELVPQ GQLGIPEVEE PHCTFVENSL AKARHASRLA
     GLPALADDSG LCVDAFGGAP GVFSARYAGE PKSDARNNEK LLSALGETAA RGARFVSVIV
     FVRHADDPQP IIAEGEWHGE ILSAARGDDG FGYDPLFYIR ELDKSAAELD AAEKNRRSHR
     GQALARLVER LQRLR
//

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