ID A0A2J6K6S8_LACSA Unreviewed; 581 AA.
AC A0A2J6K6S8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
GN ORFNames=LSAT_3X89301 {ECO:0000313|EMBL:PLY70786.1};
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY70786.1};
RN [1] {ECO:0000313|EMBL:PLY70786.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28401891; DOI=10.1038/ncomms14953;
RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT "Genome assembly with in vitro proximity ligation data and whole-genome
RT triplication in lettuce.";
RL Nat. Commun. 8:14953-14953(2017).
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 {ECO:0000256|RuleBase:RU365100}.
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:PLY70786.1}.
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DR EMBL; NBSK01008559; PLY70786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6K6S8; -.
DR STRING; 4236.A0A2J6K6S8; -.
DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_3X89301_mrna; cds-PLY70786.1; gene-LSAT_3X89301.
DR Gramene; rna-gnl|WGS:NBSK|LSAT_3X89301_mrna; cds-PLY70786.1; gene-LSAT_3X89301.
DR UniPathway; UPA00253; UER00457.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
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; 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; 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 Transferase {ECO:0000256|RuleBase:RU365100}.
FT DOMAIN 34..161
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 455..566
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 65165 MW; 688E5C3694AE9229 CRC64;
MDVKPEVNGG VKEEKHNRPP PVIDGPTNPM VTPLLNDLYQ FTMAYAYWKA GKHKERAVFD
LYFRKNPFGG EYTVFAGLEE CIRFIANFKL SKEEIAFVRE SLSPTCEDAF FDYLEGIDCS
DVEVYAIAEG SVVFPKIPLM RVEGPVAVVQ LLETPYVNLI NYASLVTTNA ARHRFVAGKS
KLLLEFGLRR AQGPDGGIGA SRYCYMGGFD ATSNCAAGKI FGIPLRGTHS HAFVSSFMGT
DEIIDKSLKS HDGSQVCEDF VGASQTWLSK IKRLSILKGV FGETNQSELA AFISYALAFP
DNFLALVDTY DVMKSGVPNF CAVALALNDL GYKARGIRLD SGDLAYLSCE TRKFFQTIET
EFVIPGFGKT GITASNDLNE ETLDALNKQA KLFIYFEFLT SVWYGHEVDA FGIGTYLVTC
YAQAALGCVF KLVEINNQPR IKLSEDVSKV SIPCKKRSFR LYGKEGYALL DIMSGENEPP
PKVGERILCR HPFNESKRAY VVPQRVEELL KCYWPGTTDK KREELPTLEQ NRERVGKQLE
QMRPDHMRRL NPTPYKVSVT AKLYDFIHFL WLNEAPVGEL Q
//
