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Database: UniProt
Entry: A0A482WDV7_9CUCU
LinkDB: A0A482WDV7_9CUCU
Original site: A0A482WDV7_9CUCU 
ID   A0A482WDV7_9CUCU        Unreviewed;       554 AA.
AC   A0A482WDV7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00021569, ECO:0000256|RuleBase:RU365100};
DE            EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
GN   ORFNames=BDFB_009531 {ECO:0000313|EMBL:RZC42839.1};
OS   Asbolus verrucosus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Pimeliinae; Asbolus.
OX   NCBI_TaxID=1661398 {ECO:0000313|EMBL:RZC42839.1, ECO:0000313|Proteomes:UP000292052};
RN   [1] {ECO:0000313|EMBL:RZC42839.1, ECO:0000313|Proteomes:UP000292052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Butters {ECO:0000313|EMBL:RZC42839.1};
RC   TISSUE=Head and leg muscle {ECO:0000313|EMBL:RZC42839.1};
RA   Rider S.D.;
RT   "Genome of the blue death feigning beetle - Asbolus verrucosus.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the first step in the biosynthesis of NAD from
CC       nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-
CC       ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
CC       Helps prevent cellular oxidative stress via its role in NAD
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00023426}.
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         ECO:0000256|RuleBase:RU365100};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|RuleBase:RU365100}.
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:RU365100}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family.
CC       {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|RuleBase:RU365100}.
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:RZC42839.1}.
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DR   EMBL; QDEB01004517; RZC42839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A482WDV7; -.
DR   STRING; 1661398.A0A482WDV7; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000292052; Unassembled WGS sequence.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01570; NAPRTase_A; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
DR   Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 2.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR041525; N/Namide_PRibTrfase.
DR   InterPro; IPR041619; NAPRTase_C.
DR   InterPro; IPR040727; NAPRTase_N.
DR   InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR   InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   NCBIfam; TIGR01513; NAPRTase_put; 1.
DR   PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF04095; NAPRTase; 1.
DR   Pfam; PF17956; NAPRTase_C; 1.
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, ECO:0000256|RuleBase:RU365100};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|RuleBase:RU365100};
KW   Reference proteome {ECO:0000313|Proteomes:UP000292052};
KW   Transferase {ECO:0000256|RuleBase:RU365100}.
FT   DOMAIN          28..155
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          325..426
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
FT   DOMAIN          430..538
FT                   /note="Nicotinate phosphoribosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17956"
SQ   SEQUENCE   554 AA;  61741 MW;  246EADAD165E4520 CRC64;
     MSQMMNGVVP SWGTPEKRLG QNCIVQPLLT DFYQITMAYA YWKAGKTQAH AVFDLFFRKN
     PFQGEFTIFA GLEECVKFLT KFSYSKSDID YIRQILPPSI EEEFYDFLGK LDARGVSLYA
     VKEGTVVFPR VPLIRVEGPL IVVQLLETTL LNLVNYASLI ATNASRFRMA AGKLKLFEFG
     LRRAQGPDGA LSASRYSYIG GFDGTSNVLA GKLFNIPVKG THAHSYVTSF NNLDELTVRI
     LAPKSGGAAV DFVNLAVKWR EKLVPIFNVM LSEASDGELA AFISFAIAFP NGFLALVDTY
     DVKKSGLLNF CAVALALHDL GYAPVGIRLD SGDLAYLSIV ARNFFTQISE KYNISSFAKL
     MIMASNDINE ETILSINEQG HAIDSFGIGT HLVTCQKQPA LGCVYKMVEI NGQARIKLSH
     DVAKVTIPGK KEVYRLYGEN GHALIDLLQI SSEDPPQVGK KVLCRHPFQE SKRAFVIPSK
     VEKLLQLYWQ DGTIYQPLPN MQEIKEKVIS SLKIVRSDIR RTLNPTPYKV SVSDDLYHYL
     HNLWLENAPI GELS
//
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