ADE_PSEAE
ID ADE_PSEAE Reviewed; 316 AA.
AC Q9I6Y4;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01962};
DE Short=ADE {ECO:0000255|HAMAP-Rule:MF_01962};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01962};
DE AltName: Full=Adenine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_01962};
DE Short=AAH {ECO:0000255|HAMAP-Rule:MF_01962};
GN OrderedLocusNames=PA0148;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 2-316 IN COMPLEX WITH ADENINE;
RP CHLOROPURINE; HYPOXANTHINE AND ZINC.
RG New York structural genomix research consortium (NYSGXRC);
RT "The crystal structure of adenosine deaminase in complex with adenine,
RT chloropurine and hypoxanthine from pseudomonas aeruginosa.";
RL Submitted (DEC-2010) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenine to
CC hypoxanthine. Plays an important role in the purine salvage pathway and
CC in nitrogen catabolism. {ECO:0000255|HAMAP-Rule:MF_01962}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenine + H(+) + H2O = hypoxanthine + NH4(+);
CC Xref=Rhea:RHEA:23688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17368, ChEBI:CHEBI:28938; EC=3.5.4.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01962};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01962, ECO:0000269|Ref.2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01962,
CC ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. Adenine deaminase type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01962}.
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DR EMBL; AE004091; AAG03538.1; -; Genomic_DNA.
DR PIR; H83625; H83625.
DR RefSeq; NP_248838.1; NC_002516.2.
DR RefSeq; WP_003112641.1; NZ_QZGE01000015.1.
DR PDB; 3OU8; X-ray; 2.51 A; A/B=2-316.
DR PDB; 3PAN; X-ray; 2.63 A; A/B=2-316.
DR PDB; 3PAO; X-ray; 2.49 A; A/B=2-316.
DR PDB; 3PBM; X-ray; 2.59 A; A/B=2-316.
DR PDBsum; 3OU8; -.
DR PDBsum; 3PAN; -.
DR PDBsum; 3PAO; -.
DR PDBsum; 3PBM; -.
DR AlphaFoldDB; Q9I6Y4; -.
DR SMR; Q9I6Y4; -.
DR STRING; 287.DR97_3105; -.
DR PaxDb; Q9I6Y4; -.
DR PRIDE; Q9I6Y4; -.
DR DNASU; 879249; -.
DR EnsemblBacteria; AAG03538; AAG03538; PA0148.
DR GeneID; 879249; -.
DR KEGG; pae:PA0148; -.
DR PATRIC; fig|208964.12.peg.154; -.
DR PseudoCAP; PA0148; -.
DR HOGENOM; CLU_039228_7_0_6; -.
DR InParanoid; Q9I6Y4; -.
DR OMA; DERLMQR; -.
DR PhylomeDB; Q9I6Y4; -.
DR BioCyc; PAER208964:G1FZ6-150-MON; -.
DR EvolutionaryTrace; Q9I6Y4; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0000034; F:adenine deaminase activity; IDA:PseudoCAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IBA:GO_Central.
DR GO; GO:0043103; P:hypoxanthine salvage; IBA:GO_Central.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01320; ADA; 1.
DR HAMAP; MF_01962; Adenine_deaminase; 1.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR028892; ADE.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43114; PTHR43114; 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 3D-structure; Hydrolase; Metal-binding; Nucleotide metabolism;
KW Reference proteome; Zinc.
FT CHAIN 1..316
FT /note="Adenine deaminase"
FT /id="PRO_0000194377"
FT ACT_SITE 197
FT /note="Proton donor"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 276
FT /ligand="substrate"
FT SITE 218
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:3PAO"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3PAO"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:3PAO"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:3PAO"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:3PAO"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 109..127
FT /evidence="ECO:0007829|PDB:3PAO"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:3PAO"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:3PAO"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:3PAO"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:3PAO"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:3PAO"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:3PAO"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 284..295
FT /evidence="ECO:0007829|PDB:3PAO"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:3PAO"
SQ SEQUENCE 316 AA; 36163 MW; EFB41B00CBFDED4A CRC64;
MYEWLNALPK AELHLHLEGT LEPELLFALA ERNRIALPWN DVETLRKAYA FNNLQEFLDL
YYAGADVLRT EQDFYDLTWA YLQKCKAQNV VHVEPFFDPQ THTDRGIPFE VVLAGIRAAL
RDGEKLLGIR HGLILSFLRH LSEEQAQKTL DQALPFRDAF IAVGLDSSEV GHPPSKFQRV
FDRARSEGFL TVAHAGEEGP PEYIWEALDL LKVERIDHGV RAFEDERLMR RLIDEQIPLT
VCPLSNTKLC VFDDMSQHTI LDMLERGVKV TVNSDDPAYF GGYVTENFHA LQQSLGMTEE
QARRLAQNSL DARLVK
