ADD_ECOLI
ID ADD_ECOLI Reviewed; 333 AA.
AC P22333; P78163; P78240;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Adenosine deaminase {ECO:0000255|HAMAP-Rule:MF_00540, ECO:0000303|PubMed:357905};
DE EC=3.5.4.4 {ECO:0000255|HAMAP-Rule:MF_00540, ECO:0000269|PubMed:1998686, ECO:0000269|PubMed:357905};
DE AltName: Full=Adenosine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_00540};
GN Name=add {ECO:0000255|HAMAP-Rule:MF_00540, ECO:0000303|PubMed:1998686};
GN OrderedLocusNames=b1623, JW1615;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=1998686; DOI=10.1021/bi00222a033;
RA Chang Z., Nygaard P., Chinault A.C., Kellems R.E.;
RT "Deduced amino acid sequence of Escherichia coli adenosine deaminase
RT reveals evolutionarily conserved amino acid residues: implications for
RT catalytic function.";
RL Biochemistry 30:2273-2280(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=357905; DOI=10.1016/s0076-6879(78)51070-7;
RA Nygaard P.;
RT "Adenosine deaminase from Escherichia coli.";
RL Methods Enzymol. 51:508-512(1978).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-
CC deoxyadenosine. {ECO:0000255|HAMAP-Rule:MF_00540,
CC ECO:0000269|PubMed:357905}.
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; EC=3.5.4.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540,
CC ECO:0000269|PubMed:1998686, ECO:0000269|PubMed:357905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540,
CC ECO:0000269|PubMed:1998686, ECO:0000269|PubMed:357905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+);
CC Xref=Rhea:RHEA:28190, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17256, ChEBI:CHEBI:28938, ChEBI:CHEBI:28997; EC=3.5.4.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540,
CC ECO:0000269|PubMed:357905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540,
CC ECO:0000269|PubMed:357905};
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-Rule:MF_00540};
CC -!- ACTIVITY REGULATION: Inhibited by reagents such as p-
CC chloromercuribenzoate, and by coformycin, a structural analog of
CC inosine. {ECO:0000269|PubMed:357905}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=75 uM for adenosine {ECO:0000269|PubMed:357905};
CC KM=40 uM for 2'-deoxyadenosine {ECO:0000269|PubMed:357905};
CC pH dependence:
CC Optimum pH is between 6.9 and 8.5 for both adenosine and 2-
CC deoxyadenosine. {ECO:0000269|PubMed:357905};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. Adenosine deaminase subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00540}.
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DR EMBL; M59033; AAA23419.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74695.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15374.1; -; Genomic_DNA.
DR PIR; A64919; A64919.
DR RefSeq; NP_416140.1; NC_000913.3.
DR RefSeq; WP_000567490.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P22333; -.
DR SMR; P22333; -.
DR BioGRID; 4260251; 30.
DR DIP; DIP-9056N; -.
DR IntAct; P22333; 15.
DR MINT; P22333; -.
DR STRING; 511145.b1623; -.
DR jPOST; P22333; -.
DR PaxDb; P22333; -.
DR PRIDE; P22333; -.
DR EnsemblBacteria; AAC74695; AAC74695; b1623.
DR EnsemblBacteria; BAA15374; BAA15374; BAA15374.
DR GeneID; 66674486; -.
DR GeneID; 945851; -.
DR KEGG; ecj:JW1615; -.
DR KEGG; eco:b1623; -.
DR PATRIC; fig|1411691.4.peg.638; -.
DR EchoBASE; EB0029; -.
DR eggNOG; COG1816; Bacteria.
DR HOGENOM; CLU_039228_0_2_6; -.
DR InParanoid; P22333; -.
DR OMA; NHFTIHA; -.
DR PhylomeDB; P22333; -.
DR BioCyc; EcoCyc:ADENODEAMIN-MON; -.
DR BioCyc; MetaCyc:ADENODEAMIN-MON; -.
DR PRO; PR:P22333; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:RHEA.
DR GO; GO:0004000; F:adenosine deaminase activity; IDA:EcoliWiki.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006154; P:adenosine catabolic process; IGI:EcoliWiki.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0046101; P:hypoxanthine biosynthetic process; IGI:EcoliWiki.
DR GO; GO:0043103; P:hypoxanthine salvage; IGI:EcoliWiki.
DR GO; GO:0046103; P:inosine biosynthetic process; IBA:GO_Central.
DR GO; GO:0015950; P:purine nucleotide interconversion; IGI:EcoliWiki.
DR GO; GO:0032261; P:purine nucleotide salvage; IGI:EcoliWiki.
DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IGI:EcoliWiki.
DR CDD; cd01320; ADA; 1.
DR HAMAP; MF_00540; A_deaminase; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR028893; A_deaminase.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11409; PTHR11409; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01430; aden_deam; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc.
FT CHAIN 1..333
FT /note="Adenosine deaminase"
FT /id="PRO_0000194367"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P03958, ECO:0000255|HAMAP-
FT Rule:MF_00540"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P03958, ECO:0000255|HAMAP-
FT Rule:MF_00540"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P03958, ECO:0000255|HAMAP-
FT Rule:MF_00540"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P03958, ECO:0000255|HAMAP-
FT Rule:MF_00540"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P03958, ECO:0000255|HAMAP-
FT Rule:MF_00540"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P03958, ECO:0000255|HAMAP-
FT Rule:MF_00540"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P03958, ECO:0000255|HAMAP-
FT Rule:MF_00540"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P03958, ECO:0000255|HAMAP-
FT Rule:MF_00540"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P03958, ECO:0000255|HAMAP-
FT Rule:MF_00540"
FT SITE 221
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P03958, ECO:0000255|HAMAP-
FT Rule:MF_00540"
FT CONFLICT 145
FT /note="Missing (in Ref. 1; AAA23419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 36397 MW; 6234BBC13C505ED6 CRC64;
MIDTTLPLTD IHRHLDGNIR PQTILELGRQ YNISLPAQSL ETLIPHVQVI ANEPDLVSFL
TKLDWGVKVL ASLDACRRVA FENIEDAARH GLHYVELRFS PGYMAMAHQL PVAGVVEAVI
DGVREGCRTF GVQAKLIGIM SRTFGEAACQ QELEAFLAHR DQITALDLAG DELGFPGSLF
LSHFNRARDA GWHITVHAGE AAGPESIWQA IRELGAERIG HGVKAIEDRA LMDFLAEQQI
GIESCLTSNI QTSTVAELAA HPLKTFLEHG IRASINTDDP GVQGVDIIHE YTVAAPAAGL
SREQIRQAQI NGLEMAFLSA EEKRALREKV AAK
