(data stored in SCRATCH zone)

SWISSPROT: Q750D3_ASHGO

ID   Q750D3_ASHGO            Unreviewed;       400 AA.
AC   Q750D3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 91.
DE   RecName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000256|RuleBase:RU362021};
DE            EC=2.7.7.1 {ECO:0000256|RuleBase:RU362021};
GN   ORFNames=AGOS_AGR022C {ECO:0000313|EMBL:AAS54511.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54511.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54511.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate
CC         + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, 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 family.
CC       {ECO:0000256|RuleBase:RU362021}.
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DR   EMBL; AE016820; AAS54511.2; -; Genomic_DNA.
DR   RefSeq; NP_986687.2; NM_211749.2.
DR   STRING; 33169.AAS54511; -.
DR   EnsemblFungi; AAS54511; AAS54511; AGOS_AGR022C.
DR   GeneID; 4622986; -.
DR   KEGG; ago:AGOS_AGR022C; -.
DR   HOGENOM; HOG000216047; -.
DR   InParanoid; Q750D3; -.
DR   KO; K06210; -.
DR   OMA; VPHGIQR; -.
DR   UniPathway; UPA00253; UER00600.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
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;
DR   PRODOM; Q750D3.
DR   SWISS-2DPAGE; Q750D3.
KW   ATP-binding {ECO:0000256|RuleBase:RU362021};
KW   NAD {ECO:0000256|RuleBase:RU362021};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362021};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU362021};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|RuleBase:RU362021};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|RuleBase:RU362021}.
FT   DOMAIN          168..358
FT                   /note="CTP_transf_like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..74
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   400 AA;  44837 MW;  197AB3A511B0A5C7 CRC64;
     MDPTRAPDFK PLQGDDKPEP PLAPDSEIPE NGPIMPFVLA DYNTSIDAPI HPKSYKKSMK
     RNSSQPSNCS KGRGGSGSIP LKRSGLEPFS NDVSSESECG EEDEQQGESH AADANSSKLR
     SMVQNIADLE EVPCGIIRQA RILEDYEFPT HRLKTTLHNA NKLPLVIVAC GSFSPITHLH
     LRMFEMAMDA IVEQTRFEVV GGYYSPVSDN YNKPGLASAT HRVRMCELAC ERTSSWLMVD
     AWESLQPQYT RTAKVLDHFN DEINVKRGGI KTSTGDRIGV KIMLLAGGDL IESMGEPNVW
     ADADLHHILG NYGCLIVERT GSDVRSFLLS HDIMYEHRRN ILVIKQMIYN DISSTKVRLF
     IRRGMSVQYL LPNSVIRYIQ EYGLYVNEHE PVQQVISNKD
//

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