ADE_KLULA
ID ADE_KLULA Reviewed; 355 AA.
AC Q6CM42;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=KLLA0E23254g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; CR382125; CAH00084.1; -; Genomic_DNA.
DR RefSeq; XP_454997.1; XM_454997.1.
DR AlphaFoldDB; Q6CM42; -.
DR SMR; Q6CM42; -.
DR STRING; 28985.XP_454997.1; -.
DR EnsemblFungi; CAH00084; CAH00084; KLLA0_E23167g.
DR GeneID; 2894386; -.
DR KEGG; kla:KLLA0_E23167g; -.
DR eggNOG; KOG1097; Eukaryota.
DR HOGENOM; CLU_039228_7_0_1; -.
DR InParanoid; Q6CM42; -.
DR OMA; RGWFRFQ; -.
DR Proteomes; UP000000598; Chromosome E.
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; 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 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..355
FT /note="Adenine deaminase"
FT /id="PRO_0000256236"
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 355 AA; 40428 MW; C7AB5F79AE851F42 CRC64;
MAKFECTDEV TNFLTELPKC EHHLHLEGTL EPELLFQLVE RNGVQLPGTF PKTVNELHVI
YNNFADLQDF LNYYYIGCNV LLSEDDFFEL AWSYFKRVST QGLRHAEVFY DPQSHTSRGI
SLEVVTKGFE RACAKAQEEF NISTKLIMCL LRHCPVEECM DTVKSAKSLI ESGVIDGLGL
DSSERPFPPE LFVECYQLAK SYNKELQLTA HAGEEGDPSF VTNTLDLLET TRIDHGVRSI
EDAELIKRLA AQKVMLTLCP LSNVKLQVVK DVSELPLQEF LDNDVPFSIN SDDPAYFGGY
ILQNYLEVYS RFGWSKAVWA KIARQSIEGS WCDPKRKQEL LSEVSEVVNK YVNLP
