(data stored in ACNUC7421 zone)

SWISSPROT: ADD_PSEHT

ID   ADD_PSEHT               Reviewed;         333 AA.
AC   Q3IF68;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 73.
DE   RecName: Full=Adenosine deaminase {ECO:0000255|HAMAP-Rule:MF_00540};
DE            EC=3.5.4.4 {ECO:0000255|HAMAP-Rule:MF_00540};
DE   AltName: Full=Adenosine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_00540};
GN   Name=add {ECO:0000255|HAMAP-Rule:MF_00540};
GN   OrderedLocusNames=PSHAa0102;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- CATALYTIC ACTIVITY: Adenosine + H(2)O = inosine + NH(3).
CC       {ECO:0000255|HAMAP-Rule:MF_00540}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00540};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Adenosine and AMP deaminases family. Adenosine
CC       deaminase subfamily. {ECO:0000255|HAMAP-Rule:MF_00540}.
DR   EMBL; CR954246; CAI85211.1; -; Genomic_DNA.
DR   RefSeq; WP_011326829.1; NC_007481.1.
DR   ProteinModelPortal; Q3IF68; -.
DR   SMR; Q3IF68; -.
DR   STRING; 326442.PSHAa0102; -.
DR   EnsemblBacteria; CAI85211; CAI85211; PSHAa0102.
DR   KEGG; pha:PSHAa0102; -.
DR   PATRIC; fig|326442.8.peg.101; -.
DR   eggNOG; ENOG4105EKD; Bacteria.
DR   eggNOG; COG1816; LUCA.
DR   HOGENOM; HOG000218815; -.
DR   KO; K01488; -.
DR   OMA; QWCGADR; -.
DR   OrthoDB; POG091H02QG; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00540; A_deaminase; 1.
DR   InterPro; IPR001365; A/AMP_deaminase_dom.
DR   InterPro; IPR028893; A_deaminase.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01430; aden_deam; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IF68.
DR   SWISS-2DPAGE; Q3IF68.
KW   Complete proteome; Hydrolase; Metal-binding; Nucleotide metabolism;
KW   Reference proteome; Zinc.
FT   CHAIN         1    333       Adenosine deaminase.
FT                                /FTId=PRO_1000017681.
FT   ACT_SITE    200    200       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00540}.
FT   METAL        12     12       Zinc; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00540}.
FT   METAL        14     14       Zinc; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00540}.
FT   METAL       197    197       Zinc; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00540}.
FT   METAL       278    278       Zinc; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00540}.
FT   BINDING      14     14       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00540}.
FT   BINDING      16     16       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00540}.
FT   BINDING     170    170       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00540}.
FT   BINDING     279    279       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00540}.
FT   SITE        221    221       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00540}.
SQ   SEQUENCE   333 AA;  36394 MW;  A15C7B710DA3C6E5 CRC64;
     MINRKLPLLD IHRHLDGNVR AQTILELGRQ FNITLPADNV AALIPHVQVI DPEPNLMAFL
     QKLDWGVTVL GDYDACRRIA IENIEDAQAQ GLDYVELRFS PYYMAQSQGL HPQGVVEAVI
     DGIKSATKGA NVKANLIGIL SRTYGVKVCQ QELDALLAFK DDLVAVDLAG DEIGFPGELF
     VEHFKQVHDA YLAATIHAGE ALGAPSIWQA INELGASRIG HGVKAIEDIE LMNYLRDKRI
     GIESCLTSNI QTSTVNDLAQ HPLKQFLDHG ILACINTDDP AVEGIEIEHE YLVAAPQAGL
     SQADIEKAQA NALEIAYLSY SDKKALLTMA STR
//

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