(data stored in SCRATCH zone)

SWISSPROT: Q2IM44_ANADE

ID   Q2IM44_ANADE            Unreviewed;       376 AA.
AC   Q2IM44;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   SubName: Full=Adenosine deaminase {ECO:0000313|EMBL:ABC79875.1};
DE            EC=3.5.4.4 {ECO:0000313|EMBL:ABC79875.1};
GN   OrderedLocusNames=Adeh_0098 {ECO:0000313|EMBL:ABC79875.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79875.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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; CP000251; ABC79875.1; -; Genomic_DNA.
DR   RefSeq; WP_011419158.1; NC_007760.1.
DR   STRING; 290397.Adeh_0098; -.
DR   EnsemblBacteria; ABC79875; ABC79875; Adeh_0098.
DR   KEGG; ade:Adeh_0098; -.
DR   eggNOG; ENOG4105EKD; Bacteria.
DR   eggNOG; COG1816; LUCA.
DR   HOGENOM; HOG000218816; -.
DR   KO; K01488; -.
DR   OMA; QWCGADR; -.
DR   BioCyc; ADEH290397:G1G5W-102-MONOMER; -.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01320; ADA; 1.
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.
PE   3: Inferred from homology;
DR   PRODOM; Q2IM44.
DR   SWISS-2DPAGE; Q2IM44.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00331575,
KW   ECO:0000313|EMBL:ABC79875.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00331580};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Zinc {ECO:0000256|SAAS:SAAS00331599}.
FT   DOMAIN       20    341       A_deaminase. {ECO:0000259|Pfam:PF00962}.
SQ   SEQUENCE   376 AA;  40729 MW;  11D52912429C07EF CRC64;
     MAQAAPTTLP QVTEALVRDL PKTDLHCHLD GSVRLATVLA LAEQQGVRLP ADTPEGLAKA
     IHMGEVCASL EDYLTAFDVT LAVLQTEEAL YRTAYELALD AAAENVRYLE VRYSPVLHTR
     KGLKPTTIVD AVLAGLRAAR RETGIESNVI ICGIRHIDPT TSVRLAELAV AYKGKGVVGF
     DLAGAEEGHP ARRHRDAVQL ILDNNVNVTI HAGEAFGPES IAQAVHWCGA HRIGHGVRLR
     ENGDLLNYLN DHRIPLEMCP SSNVQTGSVQ GFASHPLKFY FDFGLRVSVN TDNRLITDTT
     VTKELLVAHR EMGFTLEDLC TVLVQGFKSA FLPFRDKQEL LRRVNLEIAQ VLARHGAPAP
     AAGDGAARAD AGARAP
//

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