ID D7B6D1_NOCDD Unreviewed; 329 AA.
AC D7B6D1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Adenine deaminase {ECO:0000256|HAMAP-Rule:MF_01962};
DE Short=ADE {ECO:0000256|HAMAP-Rule:MF_01962};
DE EC=3.5.4.2 {ECO:0000256|HAMAP-Rule:MF_01962};
DE AltName: Full=Adenine aminohydrolase {ECO:0000256|HAMAP-Rule:MF_01962};
DE Short=AAH {ECO:0000256|HAMAP-Rule:MF_01962};
GN OrderedLocusNames=Ndas_1969 {ECO:0000313|EMBL:ADH67396.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH67396.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH67396.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
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:0000256|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:0000256|HAMAP-Rule:MF_01962};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01962};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01962};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. Adenine deaminase type 2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01962}.
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DR EMBL; CP002040; ADH67396.1; -; Genomic_DNA.
DR RefSeq; WP_013153003.1; NC_014210.1.
DR AlphaFoldDB; D7B6D1; -.
DR STRING; 446468.Ndas_1969; -.
DR KEGG; nda:Ndas_1969; -.
DR eggNOG; COG1816; Bacteria.
DR HOGENOM; CLU_039228_7_0_11; -.
DR OrthoDB; 105475at2; -.
DR Proteomes; UP000002219; Chromosome 1.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0043103; P:hypoxanthine salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01320; ADA; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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 NCBIfam; TIGR01430; aden_deam; 1.
DR PANTHER; PTHR43114; ADENINE DEAMINASE; 1.
DR PANTHER; PTHR43114:SF6; ADENINE DEAMINASE; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01962, ECO:0000313|EMBL:ADH67396.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01962};
KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01962};
KW Reference proteome {ECO:0000313|Proteomes:UP000002219};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01962}.
FT DOMAIN 4..324
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
FT ACT_SITE 192
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT SITE 213
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
SQ SEQUENCE 329 AA; 36121 MW; BB412A1C27AF2B4F CRC64;
MPIPKAELHV HIEGTLEPEL AFALARRNGL TPPHPDVDSL RRAYSFTDLQ SFLDLYYALM
DVLRTEADFT DLATAYLDRA AAQGVRHAEI FFDPQAHTGR GISLDTVVNG LTAALNTSEH
THNISTTLIL CFLRDRPAAE ALDTLHQARP HLEHISAVGL DSAEVGHPPE KFTEVFAAAR
DLGLRRVAHA GEEGPASYIW QALNLLGAER IDHGIRCLED PDLVTHLAAT QTPLTVCPLS
NVRLRAVPDL AQHPLPALME AGLLVTVNSD DPSYFGGYVH DNYQALHTHL GLGAEQLRQL
ARNSFTASFL TPQRKAQLIA EVDAHPHPW
//
