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Entry: D5V5I0_ARCNC
LinkDB: D5V5I0_ARCNC
Original site: D5V5I0_ARCNC 
ID   D5V5I0_ARCNC            Unreviewed;       334 AA.
AC   D5V5I0;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 80.
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=Arnit_1458 {ECO:0000313|EMBL:ADG93115.1};
OS   Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS   7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Arcobacteraceae; Arcobacter.
OX   NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG93115.1, ECO:0000313|Proteomes:UP000000939};
RN   [1] {ECO:0000313|EMBL:ADG93115.1, ECO:0000313|Proteomes:UP000000939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI
RC   {ECO:0000313|Proteomes:UP000000939};
RX   PubMed=21304714; DOI=10.4056/sigs.912121;
RA   Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA   Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL   Stand. Genomic Sci. 2:300-308(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; CP001999; ADG93115.1; -; Genomic_DNA.
DR   RefSeq; WP_013135260.1; NC_014166.1.
DR   AlphaFoldDB; D5V5I0; -.
DR   STRING; 572480.Arnit_1458; -.
DR   KEGG; ant:Arnit_1458; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_7_0_7; -.
DR   OMA; QHNILDM; -.
DR   OrthoDB; 105475at2; -.
DR   Proteomes; UP000000939; Chromosome.
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; ADENOSINE/ADENINE DEAMINASE-RELATED; 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:ADG93115.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01962};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000939};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01962}.
FT   DOMAIN          9..328
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
FT   ACT_SITE        197
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT   BINDING         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT   SITE            218
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
SQ   SEQUENCE   334 AA;  38636 MW;  68519306D2A18751 CRC64;
     MIEFIKKIPK AELHLHIEGS LEPELMFELA KRNNIKIPYN SVEEVRAAYD FTNLQSFLDI
     YYSGANVLLH KKDFYDLTWA YILKCVQNSI IHTEIFFDPQ THTQRGVSFD TIILGISQAL
     EDAKEKFGIT SNIIMCFLRH LSQEEALKTF EESLPFKDKI IGVGLDSSEL GHPPSKFKEV
     FKKAKDAGFK LVAHAGEEAD YSYIYEALDL LDIQRIDHGV QAVHSKELME RLKKEQTPLT
     VCPNSNIELK VFENYKQHNV KQLLDYGLNV TINSDDPAYF KGYLNDNFIN LYENIDLTKE
     DIIKLVRNSF NSSFISDELK KEYLIKLDNF LENK
//
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