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Database: UniProt
Entry: A0A364L5V5_9EURO
LinkDB: A0A364L5V5_9EURO
Original site: A0A364L5V5_9EURO 
ID   A0A364L5V5_9EURO        Unreviewed;       489 AA.
AC   A0A364L5V5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE            EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN   ORFNames=BHQ10_007210 {ECO:0000313|EMBL:RAO71198.1};
OS   Talaromyces amestolkiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO71198.1, ECO:0000313|Proteomes:UP000249363};
RN   [1] {ECO:0000313|EMBL:RAO71198.1, ECO:0000313|Proteomes:UP000249363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIB {ECO:0000313|EMBL:RAO71198.1,
RC   ECO:0000313|Proteomes:UP000249363};
RX   PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA   de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA   Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT   "Differential ?-glucosidase expression as a function of carbon source
RT   availability in Talaromyces amestolkiae: a genomic and proteomic
RT   approach.";
RL   Biotechnol. Biofuels 10:161-161(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RAO71198.1}.
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DR   EMBL; MIKG01000014; RAO71198.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A364L5V5; -.
DR   STRING; 1196081.A0A364L5V5; -.
DR   OrthoDB; 1333333at2759; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000249363; Unassembled WGS sequence.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 2.
DR   InterPro; IPR041525; N/Namide_PRibTrfase.
DR   InterPro; IPR040727; NAPRTase_N.
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   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:UP000249363}.
FT   DOMAIN          14..145
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          180..291
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
FT   DOMAIN          342..469
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
SQ   SEQUENCE   489 AA;  54757 MW;  900CE5DC6E9CCAD2 CRC64;
     MGDSPIPEGI SSLLDTDLYK LTMQCAVLKY FPDVEVTYGF TNRTPDMKLS RQAYKWLLEQ
     MERLENITIT PDEIDFLQKS CPYFNDAYLS YLRNFRLKPS QQLQIKFTPD DSTNDDDTAV
     GVLEYAVSGL WVETILYEIP LLALTSEAYF KFCDTDWNHN GQEEKAYAKG MTLLEHGCIF
     SEFGSRRRRD YHTHDLVMKG LCRAAEDAQQ KGFPGKFSGT SNVHFAMKYS VAPVGTVAHE
     WYMGIAAYTN DYENANEMGL RYWLGCFGEG VLGVALTDTF GTPAFLEAFS KPIPDYTTPS
     RGLEATFPSS AATTEINTPE SLADIKPPIS APSHHTPKQA PQKTYAQVFT GIRQDSGDPK
     NFVKLVREFY DKQGITEKKV IVFSDSLKVD NCLEYKAISE QAGFQPTFGV GTFFTNDFTK
     LSTNAKSIPL NIVIKIASAG GRPAVKLSDN LGKNTGDKQL VQEVKRRLGY VESVWEDGNE
     ATRWGKKGD
//
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