(data stored in ACNUC7421 zone)

SWISSPROT: A0KEY5_AERHH

ID   A0KEY5_AERHH            Unreviewed;       333 AA.
AC   A0KEY5;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   RecName: Full=Adenosine deaminase {ECO:0000256|HAMAP-Rule:MF_00540};
DE            EC=3.5.4.4 {ECO:0000256|HAMAP-Rule:MF_00540};
DE   AltName: Full=Adenosine aminohydrolase {ECO:0000256|HAMAP-Rule:MF_00540};
GN   Name=add-1 {ECO:0000313|EMBL:ABK37872.1};
GN   Synonyms=add {ECO:0000256|HAMAP-Rule:MF_00540};
GN   OrderedLocusNames=AHA_0273 {ECO:0000313|EMBL:ABK37872.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37872.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK37872.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC         Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938;
CC         EC=3.5.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00540,
CC         ECO:0000256|SAAS:SAAS01117141};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00540};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00540,
CC       ECO:0000256|SAAS:SAAS01080448}.
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DR   EMBL; CP000462; ABK37872.1; -; Genomic_DNA.
DR   RefSeq; WP_011704281.1; NC_008570.1.
DR   RefSeq; YP_854801.1; NC_008570.1.
DR   STRING; 380703.AHA_0273; -.
DR   EnsemblBacteria; ABK37872; ABK37872; AHA_0273.
DR   GeneID; 4490204; -.
DR   KEGG; aha:AHA_0273; -.
DR   PATRIC; fig|380703.7.peg.260; -.
DR   eggNOG; ENOG4105EKD; Bacteria.
DR   eggNOG; COG1816; LUCA.
DR   HOGENOM; HOG000218815; -.
DR   KO; K01488; -.
DR   OMA; QWCGADR; -.
DR   BioCyc; AHYD380703:G1G7B-274-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01320; ADA; 1.
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; A0KEY5.
DR   SWISS-2DPAGE; A0KEY5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00540,
KW   ECO:0000256|SAAS:SAAS00331575, ECO:0000313|EMBL:ABK37872.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00540,
KW   ECO:0000256|SAAS:SAAS00331580};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00540,
KW   ECO:0000256|SAAS:SAAS00312954};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00540, ECO:0000256|SAAS:SAAS00331599}.
FT   DOMAIN        6    326       A_deaminase. {ECO:0000259|Pfam:PF00962}.
FT   ACT_SITE    200    200       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00540}.
FT   METAL        12     12       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00540}.
FT   METAL        14     14       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00540}.
FT   METAL       197    197       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00540}.
FT   METAL       278    278       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00540}.
FT   BINDING      14     14       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00540}.
FT   BINDING      16     16       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00540}.
FT   BINDING     170    170       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00540}.
FT   BINDING     279    279       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00540}.
FT   SITE        221    221       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00540}.
SQ   SEQUENCE   333 AA;  36480 MW;  C90320411C45ADCE CRC64;
     MIDRSLPLTD LHRHLDGNIR PQTILELGRQ HNIQLPAFEL EALRPHVQIV ENEPSLVAFL
     KKLDWGVAVL ADYDACRRVA YENVEDLLRA GIDYAELRFS PAYMAMAHKL HPQGVVEAII
     DGVAAGSRDF GIKTNLIGIM SRTFGTEQCK QELDACLAHR DRLIAIDLAG DELGFPGELF
     TDHFRRVRDA GMRVTVHAGE AAGPESMWQA IRELGAERIG HGVKAIQDPA LMAYLAEHRI
     GIESCLTSNI QTTTVASLTE HPIRQFLAAG VLACLNTDDP AVEGIDLPHE YEVAAPAAGM
     TVSEIRTAQQ NGLTLAFLSE AEKAELSARA AQR
//

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