(data stored in SCRATCH zone)

SWISSPROT: C5DCW0_LACTC

ID   C5DCW0_LACTC            Unreviewed;       355 AA.
AC   C5DCW0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=Adenine deaminase {ECO:0000256|HAMAP-Rule:MF_03145};
DE            Short=ADE {ECO:0000256|HAMAP-Rule:MF_03145};
DE            EC=3.5.4.2 {ECO:0000256|HAMAP-Rule:MF_03145};
DE   AltName: Full=Adenine aminohydrolase {ECO:0000256|HAMAP-Rule:MF_03145};
DE            Short=AAH {ECO:0000256|HAMAP-Rule:MF_03145};
GN   Name=AAH1 {ECO:0000256|HAMAP-Rule:MF_03145};
GN   OrderedLocusNames=KLTH0B06226g {ECO:0000313|EMBL:CAR21621.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21621.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21621.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- FUNCTION: Catalyzes the hydrolytic deamination of adenine to
CC       hypoxanthine. Plays an important role in the purine salvage
CC       pathway and in nitrogen catabolism. {ECO:0000256|HAMAP-
CC       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;
CC         EC=3.5.4.2; Evidence={ECO:0000256|HAMAP-Rule:MF_03145};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03145};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03145};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03145}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03145}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Adenosine and AMP deaminases family. Adenine
CC       deaminase type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_03145}.
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DR   EMBL; CU928166; CAR21621.1; -; Genomic_DNA.
DR   RefSeq; XP_002552059.1; XM_002552013.1.
DR   STRING; 381046.XP_002552059.1; -.
DR   EnsemblFungi; CAR21621; CAR21621; KLTH0B06226g.
DR   GeneID; 8290898; -.
DR   KEGG; lth:KLTH0B06226g; -.
DR   HOGENOM; HOG000218813; -.
DR   InParanoid; C5DCW0; -.
DR   KO; K01488; -.
DR   OMA; DERLMQR; -.
DR   OrthoDB; 1045809at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
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/AMP_deaminase_dom.
DR   InterPro; IPR028892; ADE.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
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;
DR   PRODOM; C5DCW0.
DR   SWISS-2DPAGE; C5DCW0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03145};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03145};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03145};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03145};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03145};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_03145}.
FT   DOMAIN       17    341       A_deaminase. {ECO:0000259|Pfam:PF00962}.
FT   ACT_SITE    214    214       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_03145}.
FT   METAL        23     23       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03145}.
FT   METAL        25     25       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03145}.
FT   METAL       211    211       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03145}.
FT   METAL       292    292       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03145}.
FT   BINDING     293    293       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03145}.
FT   SITE        235    235       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03145}.
SQ   SEQUENCE   355 AA;  40408 MW;  2418BEE44975E6BD CRC64;
     MPEYECTSVM REFLHELPKC EHHVHLEGTL EPDLLYPLAL RNNVTLPNQF PKTVEELEKR
     YVMFRDLQDF LDFYYIGCEV LLQEEDFFDL AWAYFKRAHA QGLRHAEVFF DPQSHTPRGV
     AIETVVAGFK RACQKALDEL QVTSKLIMCL LRHLPVEECK ATLESSRVLF ETQQLHGLGL
     DSAEQPFPPE LFTECYELAR QFHPDVKLTA HAGEEGSAKY VSNALDLLQV TRIDHGVRSV
     EDPELVARLA RDKTMLTICP LSSLKLQVVK DISDLPLTQL LEAGVPFSIN SDDPAYFGGY
     ILDNYVAVQK KFNWDAATWA KVARQAIEGS WCDGKRKDEL LTMLAAVVDK YSALI
//

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