ADE_CANAL
ID ADE_CANAL Reviewed; 356 AA.
AC Q59ZB1; A0A1D8PHS3; Q59Z49;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_03145};
DE Short=ADE {ECO:0000255|HAMAP-Rule:MF_03145};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_03145};
DE AltName: Full=Adenine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_03145};
DE Short=AAH {ECO:0000255|HAMAP-Rule:MF_03145};
GN Name=AAH1 {ECO:0000255|HAMAP-Rule:MF_03145};
GN OrderedLocusNames=CAALFM_C206970WA; ORFNames=CaO19.2251, CaO19.9791;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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_03145}.
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_03145};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03145};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03145};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03145}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03145}.
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_03145}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AOW27697.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP017624; AOW27697.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_714841.2; XM_709748.2.
DR AlphaFoldDB; Q59ZB1; -.
DR SMR; Q59ZB1; -.
DR STRING; 237561.Q59ZB1; -.
DR GeneID; 3643529; -.
DR KEGG; cal:CAALFM_C206970WA; -.
DR CGD; CAL0000194200; AAH1.
DR eggNOG; KOG1097; Eukaryota.
DR HOGENOM; CLU_039228_7_0_1; -.
DR InParanoid; Q59ZB1; -.
DR OrthoDB; 1045809at2759; -.
DR PRO; PR:Q59ZB1; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000034; F:adenine deaminase activity; IBA:GO_Central.
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 GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR CDD; cd01320; ADA; 1.
DR HAMAP; MF_01962; Adenine_deaminase; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
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.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleotide metabolism; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..356
FT /note="Adenine deaminase"
FT /id="PRO_0000256232"
FT ACT_SITE 214
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT SITE 235
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
SQ SEQUENCE 356 AA; 40782 MW; B22B1ED9D27A9F19 CRC64;
MAQYECSEHM ENFLRELPKC EHHVHLEGTL EPSLLFKLAK RNNITLPETF PKTVEECNDR
YNRFADLQDF LDHYYIGMGV LITENDFYDL AMDYFTKAHS DGCLHSEVFF DPQGHVERNI
DIDVVVQGFN RACKDANTKY GTTNKLIMCL LRHLPAENGL QTIHSASKYY QDGIIHGLGL
DSSEKPFPPN LFTECYAHIK DNFPEVGLTA HAGEEGDHTF VSDALNLLKV SRIDHGVNSH
QSEELMQRLA EQKTLLSLCP LSNVKLQVVK DVKELPIDKF FQMNVPFSIN SDDPAYFGGY
ILDNYKAVHT RFGFTKDQWK IIALNGIKGS WCDDQRKNEL ISLVEEVYKK YNIEGC
