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ISN1_EMENI
ID   ISN1_EMENI              Reviewed;         451 AA.
AC   Q5B8A8; C8VI84;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=IMP-specific 5'-nucleotidase 1;
DE            EC=3.1.3.99 {ECO:0000250|UniProtKB:Q99312};
GN   Name=isn1; ORFNames=AN3222;
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 [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   [2]
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: IMP-specific 5'-nucleotidase involved in IMP (inositol
CC       monophosphate) degradation. {ECO:0000250|UniProtKB:Q99312}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58053; EC=3.1.3.99;
CC         Evidence={ECO:0000250|UniProtKB:Q99312};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q99312};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q99312}.
CC   -!- SIMILARITY: Belongs to the ISN1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBF83155.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA63123.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000054; EAA63123.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001306; CBF83155.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_660826.1; XM_655734.1.
DR   AlphaFoldDB; Q5B8A8; -.
DR   SMR; Q5B8A8; -.
DR   STRING; 162425.CADANIAP00009840; -.
DR   EnsemblFungi; EAA63123; EAA63123; AN3222.2.
DR   GeneID; 2874146; -.
DR   KEGG; ani:AN3222.2; -.
DR   eggNOG; ENOG502QR24; Eukaryota.
DR   HOGENOM; CLU_031816_1_0_1; -.
DR   InParanoid; Q5B8A8; -.
DR   OrthoDB; 1219919at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0050483; F:IMP 5'-nucleotidase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006190; P:inosine salvage; IBA:GO_Central.
DR   GO; GO:0071590; P:nicotinamide riboside biosynthetic process; IBA:GO_Central.
DR   GO; GO:0071592; P:nicotinic acid riboside biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR009453; ISN1.
DR   PANTHER; PTHR28213; PTHR28213; 1.
DR   Pfam; PF06437; ISN1; 2.
DR   PIRSF; PIRSF028836; ISN1; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Nucleotide metabolism; Reference proteome.
FT   CHAIN           1..451
FT                   /note="IMP-specific 5'-nucleotidase 1"
FT                   /id="PRO_0000084251"
SQ   SEQUENCE   451 AA;  50831 MW;  CD028DF61B768C34 CRC64;
     MTTRYRVEYA LKSHRRDQLI EWIKGLLAVP FVLHSQPTAV QEEDATKLAA VAHDTHQRYA
     EIFSDVERLL NDHIDHELSG AAGKSKLKLL VPTVGTFFTR LYLREAFDYQ DRQRFISRRR
     FVAPSFNDVR LILNSAQLLG LVHTKGLELV TFDGDVTLYD DGANLNADSP VIPRIIRLLQ
     QGIKVGIVTA AGYTDEAKYY ERLQGLLDVM RDASDLTDEQ RSALIVMGGE SNYLFRYDAS
     SPHRLTYVPR ENWVIGEMAT WEEEDITQLL NIAESSLRAC VANLNLPVSV LRKDRAVGVF
     PKNRGRLSRE QLEETVLVVQ NTVERSQVGS RLPFCAFNGC SPFFVSHYLR HHPPRRKYKP
     PIQPCMLISI TQPGGNDVFV DIGDKSWGVR ACQQYFGGID PSRTLHVGDQ FLSAGANDFK
     ARLASTTAWI ASPAETVQLL DELDTIQKVL A
 
 
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