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Database: UniProt
Entry: M7TE39_EUTLA
LinkDB: M7TE39_EUTLA
Original site: M7TE39_EUTLA 
ID   M7TE39_EUTLA            Unreviewed;       487 AA.
AC   M7TE39;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE            EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN   ORFNames=UCREL1_4844 {ECO:0000313|EMBL:EMR68161.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS   armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR68161.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT   EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
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|ARBA:ARBA00001240};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004952}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family.
CC       {ECO:0000256|ARBA:ARBA00010897}.
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DR   EMBL; KB706303; EMR68161.1; -; Genomic_DNA.
DR   RefSeq; XP_007792760.1; XM_007794569.1.
DR   AlphaFoldDB; M7TE39; -.
DR   STRING; 1287681.M7TE39; -.
DR   KEGG; ela:UCREL1_4844; -.
DR   eggNOG; KOG2511; Eukaryota.
DR   HOGENOM; CLU_030991_0_0_1; -.
DR   OMA; IEHCLEY; -.
DR   OrthoDB; 1333333at2759; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000012174; Unassembled WGS sequence.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01401; PncB_like; 1.
DR   Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 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; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF04095; NAPRTase; 2.
DR   Pfam; PF17767; NAPRTase_N; 1.
DR   PIRSF; PIRSF000484; NAPRT; 1.
DR   SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR   SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000313|EMBL:EMR68161.1};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW   Transferase {ECO:0000313|EMBL:EMR68161.1}.
FT   DOMAIN          18..151
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          187..297
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
FT   DOMAIN          327..456
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
FT   REGION          307..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  53945 MW;  31B512E7AB412538 CRC64;
     MIEFNSSNPF PEGVNSFLDT DLYKLTMQCA VLKYYPDVPV TYAFTNRTPE KKLSRKAFSW
     LCDQISKLGN ISLSDEELRF LKEHCKYLSP AYLDFLKDFR LSPREQLKPT FHPVNGTEDN
     NSDDDVIGDI HIEIRGKWVE TILYEIPLLA LASEAYFKFM DTDWNYAGQE QKAYDKGMRL
     LEAGCVASEF GTRRRRDYHT QALVFRGLVR ANRDGEARGL PGKISGTSNV HLAMRFNIPP
     VGTVAHEWFM GIAAITDDYG GANEEALRRW VGCFGEGVLG IALTDTFGTP AFLRAFAKPI
     QYLPGTPNIP LSPHESEGEK TETKTTSSKT YADVFAGVRQ DSGDPAGFVR QMRDFYAGRG
     IRPQDKTIVF SDALDIDKCI RYKRISEEAG LRPTFGVGTF LTNDFVQLST GKKSVPLNIV
     IKISSAAGNP AVKISDNIGK NTGDATKVGQ VKRELGYVEK DWAGGDETAR WGKEDGGAAG
     KEAAAAV
//
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