(data stored in ACNUC7421 zone)

SWISSPROT: E3J3E3_FRAIE

ID   E3J3E3_FRAIE            Unreviewed;       329 AA.
AC   E3J3E3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 46.
DE   SubName: Full=Adenosine deaminase {ECO:0000313|EMBL:ADP78145.1};
DE            EC=3.5.4.4 {ECO:0000313|EMBL:ADP78145.1};
GN   OrderedLocusNames=FraEuI1c_0057 {ECO:0000313|EMBL:ADP78145.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78145.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78145.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|SAAS:SAAS00613168};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Adenosine and AMP deaminases family.
CC       {ECO:0000256|SAAS:SAAS01089805}.
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DR   EMBL; CP002299; ADP78145.1; -; Genomic_DNA.
DR   RefSeq; WP_013421268.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0057; -.
DR   EnsemblBacteria; ADP78145; ADP78145; FraEuI1c_0057.
DR   KEGG; fri:FraEuI1c_0057; -.
DR   eggNOG; ENOG4105EKD; Bacteria.
DR   eggNOG; COG1816; LUCA.
DR   HOGENOM; HOG000218814; -.
DR   KO; K01488; -.
DR   OMA; GVRCSIN; -.
DR   OrthoDB; 554648at2; -.
DR   BioCyc; FSP298654:G1GOT-57-MONOMER; -.
DR   Proteomes; UP000002484; Chromosome.
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:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR001365; A/AMP_deaminase_dom.
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.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; E3J3E3.
DR   SWISS-2DPAGE; E3J3E3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00331575,
KW   ECO:0000313|EMBL:ADP78145.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00331580};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484};
KW   Zinc {ECO:0000256|SAAS:SAAS00331599}.
FT   DOMAIN       63    314       A_deaminase. {ECO:0000259|Pfam:PF00962}.
SQ   SEQUENCE   329 AA;  34879 MW;  4311AA4B7ED9726E CRC64;
     MRDLRALPKG HLHLHFELGM RPSTLADLAA RNGVPTPPTT GFTEFGGFGV VIGGILPMFR
     EVADFERLVD EVVEDAAQEG VVYLEPSFYP YPYLDVFGTA EAAWETVLAR SALAAERHGV
     TVRWMAAVDR VFDTPAQAVE VAKLAVRNRD AGVVALGLHN DENGYPPEPF ADAFRYAKDA
     GLLSTPHAGE LDGPASVRGA IDVLLADRLQ HGIRAVEDPA LVEVLAARGT VLDVCPTSNL
     QLSVVPSLAE HPLPELLAAG VRCSINADDP LLFGPSILRE YELCRDAFGL DDELLATCAR
     SSVTGGAAPA EVQATALAGI DAWLAAPAG
//

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