ADD1_STRCO
ID ADD1_STRCO Reviewed; 396 AA.
AC Q9AK25;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Adenosine deaminase 1 {ECO:0000255|HAMAP-Rule:MF_00540, ECO:0000303|PubMed:21511036};
DE Short=ADA 1 {ECO:0000305};
DE EC=3.5.4.4 {ECO:0000255|HAMAP-Rule:MF_00540, ECO:0000269|PubMed:21511036};
DE AltName: Full=Adenosine aminohydrolase 1 {ECO:0000255|HAMAP-Rule:MF_00540};
GN Name=add1 {ECO:0000255|HAMAP-Rule:MF_00540}; Synonyms=add5;
GN OrderedLocusNames=SCO4901; ORFNames=2SCK8.27;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=21511036; DOI=10.1016/j.pep.2011.04.003;
RA Pornbanlualap S., Chalopagorn P.;
RT "Adenosine deaminase from Streptomyces coelicolor: recombinant expression,
RT purification and characterization.";
RL Protein Expr. Purif. 78:167-173(2011).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-
CC deoxyadenosine. {ECO:0000255|HAMAP-Rule:MF_00540,
CC ECO:0000269|PubMed:21511036}.
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:21511036};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540,
CC ECO:0000269|PubMed:21511036};
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:21511036};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540,
CC ECO:0000269|PubMed:21511036};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540,
CC ECO:0000269|PubMed:21511036};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00540};
CC -!- ACTIVITY REGULATION: Coformycin and 2'-deoxycoformycin, whose
CC structures mimic the transition state of the deamination reaction, are
CC potent competitive inhibitors. {ECO:0000269|PubMed:21511036}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29 uM for adenosine {ECO:0000269|PubMed:21511036};
CC KM=560 uM for 2'-deoxyadenosine {ECO:0000269|PubMed:21511036};
CC Vmax=15.4 umol/min/mg enzyme with adenosine as substrate
CC {ECO:0000269|PubMed:21511036};
CC Vmax=2.7 umol/min/mg enzyme with 2'-deoxyadenosine as substrate
CC {ECO:0000269|PubMed:21511036};
CC Note=kcat is 11.5 sec(-1) with adenosine as substrate.
CC {ECO:0000269|PubMed:21511036};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21511036}.
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; AL939121; CAC33066.1; -; Genomic_DNA.
DR RefSeq; NP_629054.1; NC_003888.3.
DR RefSeq; WP_003974072.1; NZ_VNID01000016.1.
DR AlphaFoldDB; Q9AK25; -.
DR SMR; Q9AK25; -.
DR STRING; 100226.SCO4901; -.
DR GeneID; 1100342; -.
DR KEGG; sco:SCO4901; -.
DR PATRIC; fig|100226.15.peg.4980; -.
DR eggNOG; COG1816; Bacteria.
DR HOGENOM; CLU_039228_0_0_11; -.
DR InParanoid; Q9AK25; -.
DR OMA; NHFTIHA; -.
DR PhylomeDB; Q9AK25; -.
DR Proteomes; UP000001973; 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 HAMAP; MF_00540; A_deaminase; 1.
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.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc.
FT CHAIN 1..396
FT /note="Adenosine deaminase 1"
FT /id="PRO_0000194391"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 227
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT SITE 248
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
SQ SEQUENCE 396 AA; 43961 MW; 5426A20DAB5F929E CRC64;
MTSRSTEKSA AANPAAVSKT PSPDRIRRAP KVLLHDHLDG GLRPGTIVEL ARETGYGDLP
ETDADLLGTW FRQAADSGSL ERYLETFSHT VGVMQTRDAL VRVAAECAED LAEDGVVYAE
VRYAPEQHLE KGLTLEEVVE AVNEGFREGE RRARDNGHRI RVGALLTAMR HAARSLEIAE
LANRYRDLGV VGFDIAGAEA GYPPTRHLDA FEYLKRENNH FTIHAGEAFG LPSIWQALQW
CGADRLGHGV RIIDDIQVHE DGSVKLGRLA SYVRDKRIPL ELCPSSNLQT GAADSYAEHP
IGLLRRLHFR ATVNTDNRLM SHTSMSREFE HLVEAFGYTL DDMQWFSVNA MKSAFIPFDE
RLAMINDVIK PGYAELKSEW LFQQTASTSG SSESDG
