ADD_SHESA
ID ADD_SHESA Reviewed; 331 AA.
AC A0L2R5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Shewana3_4117;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-
CC deoxyadenosine. {ECO:0000255|HAMAP-Rule:MF_00540}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191;
CC Evidence={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-Rule:MF_00540};
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; CP000469; ABK50334.1; -; Genomic_DNA.
DR RefSeq; WP_011718822.1; NC_008577.1.
DR AlphaFoldDB; A0L2R5; -.
DR SMR; A0L2R5; -.
DR STRING; 94122.Shewana3_4117; -.
DR EnsemblBacteria; ABK50334; ABK50334; Shewana3_4117.
DR GeneID; 58508583; -.
DR KEGG; shn:Shewana3_4117; -.
DR eggNOG; COG1816; Bacteria.
DR HOGENOM; CLU_039228_0_2_6; -.
DR OMA; NHFTIHA; -.
DR OrthoDB; 554648at2; -.
DR Proteomes; UP000002589; Chromosome.
DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:RHEA.
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 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 3: Inferred from homology;
KW Hydrolase; Metal-binding; Nucleotide metabolism; Zinc.
FT CHAIN 1..331
FT /note="Adenosine deaminase"
FT /id="PRO_1000017700"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT SITE 221
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
SQ SEQUENCE 331 AA; 36119 MW; 1163EEE7875551F8 CRC64;
MINTSIPLVD LHRHLDGNVR VNTIWELGHQ HGIALPADSL ETLAPFVQIQ GKETSLVAFL
KKLDWMVAVL ADLDAVKRVA YENVADAALS GLDYAELRFS PYYMAMNHKL PIEGVVEAVI
DGVKAGLKDY QVKINLIGIM SRSFGQAACT QELEGLLAHK QHLVAMDLAG DELGFPGELF
NEHFKRVRDA GLAITAHAGE AAGSQSMWQA IQELGATRIG HGVNAIHDPK LMEYLAKHRI
GIESCPTSNL HTSTVSSYAE HPFRTFMDAG VLISLNTDDP GVSAIDIKHE YRIAKSELGL
SDAELAQVQR NGVEMAFLSE SERKALYAAK A
