(data stored in SCRATCH zone)

SWISSPROT: Q75BW1_ASHGO

ID   Q75BW1_ASHGO            Unreviewed;       430 AA.
AC   Q75BW1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 103.
DE   RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|RuleBase:RU003838};
DE            EC=6.3.4.21 {ECO:0000256|RuleBase:RU003838};
GN   ORFNames=AGOS_ACR160C {ECO:0000313|EMBL:AAS51386.1};
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:AAS51386.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51386.1, 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   -!- FUNCTION: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide
CC       from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of
CC       ATP. {ECO:0000256|RuleBase:RU003838}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O +
CC         nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide +
CC         phosphate; Xref=Rhea:RHEA:36163, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32544, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:456216; EC=6.3.4.21;
CC         Evidence={ECO:0000256|RuleBase:RU003838};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1.
CC       {ECO:0000256|RuleBase:RU003838}.
CC   -!- PTM: Transiently phosphorylated on a His residue during the reaction
CC       cycle. Phosphorylation strongly increases the affinity for substrates
CC       and increases the rate of nicotinate D-ribonucleotide production.
CC       Dephosphorylation regenerates the low-affinity form of the enzyme,
CC       leading to product release. {ECO:0000256|RuleBase:RU003838}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family.
CC       {ECO:0000256|RuleBase:RU003838}.
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DR   EMBL; AE016816; AAS51386.1; -; Genomic_DNA.
DR   RefSeq; NP_983562.1; NM_208915.1.
DR   STRING; 33169.AAS51386; -.
DR   EnsemblFungi; AAS51386; AAS51386; AGOS_ACR160C.
DR   GeneID; 4619694; -.
DR   KEGG; ago:AGOS_ACR160C; -.
DR   HOGENOM; HOG000284928; -.
DR   InParanoid; Q75BW1; -.
DR   KO; K00763; -.
DR   OMA; GTSNVHF; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR   GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
DR   HAMAP; MF_00570; NAPRTase; 1.
DR   InterPro; IPR041525; N/Namide_PRibTrfase.
DR   InterPro; IPR040727; NAPRTase_N.
DR   InterPro; IPR006406; Nic_PRibTrfase.
DR   InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   PANTHER; PTHR11098; PTHR11098; 1.
DR   Pfam; PF04095; NAPRTase; 1.
DR   Pfam; PF17767; NAPRTase_N; 1.
DR   PIRSF; PIRSF000484; NAPRT; 1.
DR   SUPFAM; SSF51690; SSF51690; 1.
DR   TIGRFAMs; TIGR01514; NAPRTase; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75BW1.
DR   SWISS-2DPAGE; Q75BW1.
KW   Ligase {ECO:0000256|RuleBase:RU003838};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|RuleBase:RU003838};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          12..141
FT                   /note="NAPRTase_N"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          175..413
FT                   /note="NAPRTase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
SQ   SEQUENCE   430 AA;  48835 MW;  B180AB16720B0E6F CRC64;
     MTSEEAAIKS LLDTDMYKLT MHAAVYVNFP DTEVVYKYTN RSAGLSFNKA AIVWLEDQVS
     KLATLRFTAE EVAYLKETLP FLPAQYIDYI SSPECRMDPA TQVQLLHEQR EGEERYDLNI
     TVTGLWKDTI LYEIHMLALI SEAYFKFVDT DWVLDGQVEQ AYRKTRLLLD NGLVFSEFGT
     RRRRSLLVQD LVLQGIAEAV ADSGTGDTQF IGTSNVYFAK KYGVKPVGTV AHEWYMGIAA
     LTDDYRNANK NAMDFWLNTF GSEQAGLVLT DTFGTDTFLP MFRPPYSDVY DGVRQDSGDP
     AVFTEKVAHH YLNVLHYPRF SKVICYSDSL NPEKALQYAE VARAHGMRAS FGIGTNFTND
     FRRHSAPDAK SEPLNIVFKL LTVNGRPAIK ISDDLGKTMG DPEKVEEVKR ELGYIERTWE
     GSDEAHRWKD
//

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