ADE_EMENI
ID ADE_EMENI Reviewed; 364 AA.
AC Q8X1T6; C8V2S4; Q5B052;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
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; Synonyms=nadA; ORFNames=AN6078;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC TISSUE=Mycelium;
RX PubMed=14643670; DOI=10.1016/j.jmb.2003.10.005;
RA Ribard C., Rochet M., Labedan B., Daignan-Fornier B., Alzari P.,
RA Scazzocchio C., Oestreicher N.;
RT "Sub-families of alpha/beta barrel enzymes: a new adenine deaminase
RT family.";
RL J. Mol. Biol. 334:1117-1131(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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. Has no activity with adenosine as a substrate.
CC {ECO:0000255|HAMAP-Rule:MF_03145, ECO:0000269|PubMed:14643670}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=290 uM for adenine {ECO:0000269|PubMed:14643670};
CC Vmax=200 nmol/min/mg enzyme {ECO:0000269|PubMed:14643670};
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; AF123460; AAL56636.1; -; Genomic_DNA.
DR EMBL; AACD01000104; EAA58053.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF70232.1; -; Genomic_DNA.
DR RefSeq; XP_663682.1; XM_658590.1.
DR AlphaFoldDB; Q8X1T6; -.
DR SMR; Q8X1T6; -.
DR STRING; 162425.CADANIAP00006939; -.
DR EnsemblFungi; CBF70232; CBF70232; ANIA_06078.
DR EnsemblFungi; EAA58053; EAA58053; AN6078.2.
DR GeneID; 2870856; -.
DR KEGG; ani:AN6078.2; -.
DR VEuPathDB; FungiDB:AN6078; -.
DR eggNOG; KOG1097; Eukaryota.
DR HOGENOM; CLU_039228_7_0_1; -.
DR InParanoid; Q8X1T6; -.
DR OMA; NHFTIHA; -.
DR OrthoDB; 1045809at2759; -.
DR BRENDA; 3.5.4.2; 517.
DR SABIO-RK; Q8X1T6; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IDA:UniProtKB.
DR GO; GO:0043103; P:hypoxanthine salvage; IBA:GO_Central.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IEP:AspGD.
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 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleotide metabolism; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..364
FT /note="Adenine deaminase"
FT /id="PRO_0000256234"
FT ACT_SITE 224
FT /note="Proton donor"
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 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT SITE 244
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
SQ SEQUENCE 364 AA; 40812 MW; 2457E4B365402B35 CRC64;
MCPPNTPYQS QWHAFLHSLP KCEHHVHLEG CLEPPLIFSM ARKNNVSLPS PSSNPAYTSV
ETLSKRYGHF SSLDDFLSFY FIGMTVLKTQ SDFAELAWTY FKRAHAEGVH HTEVFFDPQV
HMERGLEYRV IVDGYVDGCK RAEKELGIST RLIMCFLKHL PLESAQRLYD TALNEGDLGL
DGRNPVIHGL GASSSEVGPP KDLFRPIYLG AKEKSINLTA HAGEEGDASY IAAALDMGAT
RIDHGIRLGE DPELMERVAR EEVLLTVCPV SNLQLKCVKS VAEVPIRKFL DAGVRFSINS
DDPAYFGAYI LECYCAVQEA FNLSVADWRL IAENGVKGSW IGEERKNELL WRIDECVKRF
EGVL
