ADD_SALTY
ID ADD_SALTY Reviewed; 333 AA.
AC Q8ZPL9;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
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}; OrderedLocusNames=STM1463;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2] {ECO:0007744|PDB:6N9M}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH 2'-DEOXYCOFORMYCIN
RP AND ZINC, AND COFACTOR.
RA Maltseva N., Kim Y., Grimshaw S., Joachimiak A.;
RT "Crystal structure of adenosine deaminase from Salmonella typhimurium
RT complexed with pentostatin (deoxycoformycin) (CASP target).";
RL Submitted (DEC-2018) to the PDB data bank.
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 ECO:0000269|Ref.2};
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; AE006468; AAL20385.1; -; Genomic_DNA.
DR RefSeq; NP_460426.1; NC_003197.2.
DR RefSeq; WP_000565569.1; NC_003197.2.
DR PDB; 6N9M; X-ray; 1.45 A; A=1-333.
DR PDBsum; 6N9M; -.
DR AlphaFoldDB; Q8ZPL9; -.
DR SMR; Q8ZPL9; -.
DR STRING; 99287.STM1463; -.
DR PaxDb; Q8ZPL9; -.
DR EnsemblBacteria; AAL20385; AAL20385; STM1463.
DR GeneID; 1252981; -.
DR KEGG; stm:STM1463; -.
DR PATRIC; fig|99287.12.peg.1546; -.
DR HOGENOM; CLU_039228_0_2_6; -.
DR OMA; NHFTIHA; -.
DR PhylomeDB; Q8ZPL9; -.
DR BioCyc; SENT99287:STM1463-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:RHEA.
DR GO; GO:0004000; F:adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006154; P:adenosine catabolic process; IBA:GO_Central.
DR GO; GO:0043103; P:hypoxanthine salvage; IBA:GO_Central.
DR GO; GO:0046103; P:inosine biosynthetic process; IBA:GO_Central.
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; 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 3D-structure; Hydrolase; Metal-binding; Nucleotide metabolism;
KW Reference proteome; Zinc.
FT CHAIN 1..333
FT /note="Adenosine deaminase"
FT /id="PRO_0000194384"
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 ECO:0000269|Ref.2, ECO:0007744|PDB:6N9M"
FT BINDING 14..16
FT /ligand="2'-deoxycoformycin"
FT /ligand_id="ChEBI:CHEBI:41829"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6N9M"
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 ECO:0000269|Ref.2, ECO:0007744|PDB:6N9M"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 141
FT /ligand="2'-deoxycoformycin"
FT /ligand_id="ChEBI:CHEBI:41829"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6N9M"
FT BINDING 170
FT /ligand="2'-deoxycoformycin"
FT /ligand_id="ChEBI:CHEBI:41829"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6N9M"
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 ECO:0000269|Ref.2, ECO:0007744|PDB:6N9M"
FT BINDING 200
FT /ligand="2'-deoxycoformycin"
FT /ligand_id="ChEBI:CHEBI:41829"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6N9M"
FT BINDING 221
FT /ligand="2'-deoxycoformycin"
FT /ligand_id="ChEBI:CHEBI:41829"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6N9M"
FT BINDING 278
FT /ligand="2'-deoxycoformycin"
FT /ligand_id="ChEBI:CHEBI:41829"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6N9M"
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 ECO:0000269|Ref.2, ECO:0007744|PDB:6N9M"
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"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:6N9M"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:6N9M"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:6N9M"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:6N9M"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:6N9M"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:6N9M"
FT STRAND 193..202
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:6N9M"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:6N9M"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:6N9M"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:6N9M"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 302..314
FT /evidence="ECO:0007829|PDB:6N9M"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:6N9M"
SQ SEQUENCE 333 AA; 36236 MW; ACA71D75A37EA1D4 CRC64;
MIDITLPLTD IHRHLDGNIR AQTILDLGRQ FNIALPAQTL ETLIPHVQVT STEPDLVSFL
TKLDWGVKVL ASLDACRRVA FENIEDAARN GLHYVELRFS PGYMAMAHQL PIAGVVEAVI
DGVRDGCNTF GVEARLIGIM SRTFGEAACL QELDALLAHR ENITALDLAG DELGFPGSLF
LSHFNRARDA GWHITVHAGE AAGPESIWQA IRELGAERIG HGVKAVEDRA LMDFLAQQRI
GIESCLTSNI QTSTVASLAD HPLKTFLEHG VLASLNTDDP AVQGVDIIHE YHVAAPAAGL
SREQIRQAQI NGLEIAFLSD SEKRALREKV AEA
