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Database: UniProt
Entry: A0A0S7DE56_9EURO
LinkDB: A0A0S7DE56_9EURO
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ID   A0A0S7DE56_9EURO        Unreviewed;       288 AA.
AC   A0A0S7DE56;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   31-JUL-2019, entry version 12.
DE   RecName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000256|RuleBase:RU362021};
DE            EC=2.7.7.1 {ECO:0000256|RuleBase:RU362021};
GN   ORFNames=ALT_0582 {ECO:0000313|EMBL:GAQ03261.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GAQ03261.1, ECO:0000313|Proteomes:UP000051487};
RN   [1] {ECO:0000313|EMBL:GAQ03261.1, ECO:0000313|Proteomes:UP000051487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GAQ03261.1,
RC   ECO:0000313|Proteomes:UP000051487};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Aspergillus lentulus strain IFM 54703T.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) =
CC         diphosphate + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57540; EC=2.7.7.1;
CC         Evidence={ECO:0000256|RuleBase:RU362021};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       nicotinamide D-ribonucleotide: step 1/1.
CC       {ECO:0000256|RuleBase:RU362021}.
CC   -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
CC       family. {ECO:0000256|RuleBase:RU362021}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GAQ03261.1}.
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DR   EMBL; BCLY01000001; GAQ03261.1; -; Genomic_DNA.
DR   EnsemblFungi; GAQ03261; GAQ03261; ALT_0582.
DR   OrthoDB; 1308027at2759; -.
DR   UniPathway; UPA00253; UER00600.
DR   Proteomes; UP000051487; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR005248; NadD/NMNAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR00482; TIGR00482; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362021};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051487};
KW   NAD {ECO:0000256|RuleBase:RU362021};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362021};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU362021,
KW   ECO:0000313|EMBL:GAQ03261.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|RuleBase:RU362021};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051487};
KW   Transferase {ECO:0000256|RuleBase:RU362021,
KW   ECO:0000313|EMBL:GAQ03261.1}.
FT   DOMAIN       49    236       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   REGION        1     27       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      267    288       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   288 AA;  32312 MW;  D3F5B527E1CD92D4 CRC64;
     MTDMVGGQSD DVHQVPPPLP PAPMENYTFP EHRLKRKMDD PEKTPLLLVA CGSFSPITYL
     HLRMFEMAAD YVKFSTDFEL IGGYLSPVSD AYRKAGLASA EHRVAMCQLA VDQTSNWLMV
     DTWEPMQKEY QPTAVVLDHF DHEINVVREG IDAGNGTRKP VRVALLAGAD LIHTMSTPGV
     WSEKDLDHIL GKYGSFIVER SGTDIDEALA ALQPWKDNIY VIQQLIQNDV SSTKIRLFLR
     REMSVRYLIP VPVIHYIEQH HLYEDDSTTA ASSSADKGKE PSQPEKSG
//
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